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  • 1.
    Andersson, M Gunnar
    et al.
    Jämförande fysiologi.
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Analysis of chitinase expression in the crayfish plague fungus Aphanomyces astaci.2002In: Dis Aquat Organ, ISSN 0177-5103, Vol. 51, no 2, p. 139-47Article in journal (Other scientific)
  • 2.
    Andersson, M Gunnar
    et al.
    Jämförande fysiologi.
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Pumilio homologue from saprolegnia parasitica specifically expressed in undifferentiated spore cysts.2002In: Eukaryot Cell, ISSN 1535-9778, Vol. 1, no 1, p. 105-11Article in journal (Other scientific)
  • 3.
    Aspan, A
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Huang, TS
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    CDNA CLONING OF PROPHENOLOXIDASE FROM THE FRESH-WATER CRAYFISH PACIFASTACUS-LENIUSCULUS AND ITS ACTIVATION1995In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 92, no 4, p. 939-943Article in journal (Refereed)
    Abstract [en]

    Prophenoloxidase (proPO), an enzyme that is the terminal component of the so-called proPO activating system, a defense and recognition system in crustaceans and insects, has been purified and cloned from a crayfish blood cell cDNA library. The deduced ami

  • 4. Ballesteros, I.
    et al.
    Martin, M.P.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Telleria, M.T.
    Dieguez-Uribeondo, J.
    Lack of specificity of the molecular diagnosis method for identification of Aphanomyces astaci2007In: BFPP-CONNAISSANCE ET GESTION DU PATRIMOINE AQUATIQUE, ISSN 1297-6318, no 385, p. 17-24Article in journal (Refereed)
    Abstract [en]

    A recent PCR-test developed for identification of Aphanomyces astaci, the organism responsible for crayfish plague, provided false positives for Aphanomyces frigidophilus, Aphanomyces repetans, and some Saprolegnia spp. Real-time PCR showed that with the designed primers, A. astaci and A. frigidophilus cannot be distinguished. The results of this study show that this particular crayfish plague PCR-test ought to be improved and that molecular-based techniques need to be contrasted to histological evidences and disease history.

  • 5.
    Bangyeekhun, E
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Molecular cloning and characterization of two serine proteinase genes from the crayfish plague fungus, Aphanomyces astaci2001In: Journal of Invertebrate Pathology, ISSN 0022-2011, E-ISSN 1096-0805, Vol. 77, no 3, p. 206-216Article in journal (Refereed)
    Abstract [en]

     

    Two novel genes encoding the serine proteinases, subtilisin (AaSP1) and trypsin (AaSP2), from Aphanomyces astaci were identified. Based on the amino acidconsensus sequences around the catalytic triad of these serine proteinases, degenerated oligonucleotides were designed for isolation of serine proteinase genes from a genomic DNA library. The AaSP1 gene encodes a full-length protein of 515 amino acids as a large precursor of 56 kDa. After cleavage of a predicted leader sequence of 18 residues and a prepeptide of 133 amino acids, the mature enzyme of 364 amino acids is generated with a calculated molecular mass of 39 kDa and a pI of 6.0. The primary sequence of AaSP1 showed similarity to both bacterial subtilisin and fungal subtilisin-like serine proteinases. Southern blot analysis of AaSP1 revealed the presence of at least two subtilisin genes in the A. astaci genome. Northern blot analysis indicated that the size of AaSP1 transcript was 1.6 kb. The AaSP2 gene encodes a prepropeptide of 276 amino acids with a molecular mass of 29 kDa. A mature protein of 237 amino acids is probably generated after cleavage of a 17-residue signal peptide and a 21-amino-acid prepeptide with a predicted molecular mass of 25 kDa and a pI of 6.0. The primary sequence of AaSP2 showed similarity to trypsin enzymes from various organisms. Southern blot analysis revealed the presence of multiple trypsin genes in the A. astaci genome. Northern blot analysis indicated that the size of AaSP2 transcript was 1.0 kb. The regulation of AaSP2 transcription was not controlled by nitrogen catabolic repression. However, the expression of AaSP2 was found to be specifically induced by crayfish plasma, implying a role in pathogenesis toward the crayfish host.

  • 6.
    Bangyeekhun, E
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Ryynänen, H J
    Henttonen, P
    Huner, J V
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Sequence analysis of the ribosomal internal transcribed spacer DNA of the crayfish parasite Psorospermium haeckeli.2001In: Diseases of Aquatic Organisms, ISSN 0177-5103, E-ISSN 1616-1580, Vol. 46, no 3, p. 217-22Article in journal (Refereed)
    Abstract [en]

    Two morphotypes of the crayfish parasite Psorospermium haeckeli were isolated from 2 crayfish species of different geographical origin. The oval-shaped sporocysts were obtained from the epidermal and connective tissue beneath the carapace of the noble crayfish Astacus astacus fromSweden and Finland. Elongated spores were isolated from the abdominal muscle tissue of the red swamp crayfish Procambarus clarkii from USA. To compare genetic divergence of 2 morphotypes of the parasite, the ribosomal internal transcribed spacer (ITS) DNA (ITS 1 and ITS 2) and the 5.8S rRNAgene were cloned and sequenced. The analysed region is variable in length, with the ribosomal ITS sequence of the European morphotype longer than the North American one. Sequence diversity is found mainly in ITS 1 and ITS 2 regions, and there is 66% and 58% similarity between the 2 morphotypes,respectively. Thus, analysis of the ribosomal ITS DNA suggests that P. haeckeli forms obtained from Europe and North America are genetically diverse, which supports the previously reported morphological characteristics.

  • 7. Bangyeekhun, Eakaphun
    et al.
    Pylkkä, Päivi
    Vennerström, Pia
    Kuronen, Henry
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Prevalence of a single fish-pathogenic Saprolegnia sp. clone in Finland and Sweden.2003In: Dis Aquat Organ, ISSN 0177-5103, Vol. 53, no 1, p. 47-53Article in journal (Refereed)
  • 8.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Andersson, M. Gunnar
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, The Linnaeus Centre for Bioinformatics.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Aphanomyces astaci and crustaceans.2009In: Oomycete Genetics and Genomics.: Diversity, Interactions, and Research Tools. / [ed] Kurt Lamour and Sophien Kamoun, Hoboken, New Jersey: John Wiley & Sons, Inc. , 2009, p. 425-433Chapter in book (Other academic)
  • 9.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Babu, Ramesh
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Jiravanichpaisal, Pikul
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    In vitro effects on bacterial growth of phenoloxidase reaction products2010In: Journal of Invertebrate Pathology, ISSN 0022-2011, E-ISSN 1096-0805, Vol. 103, no 1, p. 21-23Article in journal (Refereed)
    Abstract [en]

    An active phenoloxidase preparation from the freshwater crayfish Pacifastacus leniusculus exhibited a strong antibacterial effect in vitro on the bacteria Aeromonas hydrophila, Escherichia coli, Streptococcus pneumoniae whereas a weaker but still significant effect against Bacillus cereus, Pseudomonas aeruginosa and Staphylococcus aureus. In most cases reduction of bacterial growth was stronger when dopamine was used as substrate as compared to L-dopa. The effect on bacteria was abolished if no substrate was available for the phenoloxidase or in the presence of the phenoloxidase inhibitor phenylthiourea.

  • 10.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. Jämförande fysiologi.
    Bangyeekhun, Eakaphun
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. Jämförande fysiologi.
    Keyser, Pia
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology. jämförande fysiologi.
    Host prophenoloxidase expression in freshwater crayfish is linked to increased resistance to the crayfish plague fungus, Aphanomyces astaci.2003In: Cell Microbiol, ISSN 1462-5814, Vol. 5, no 5, p. 353-7Article in journal (Refereed)
  • 11.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Haipeng, Liu
    State Key Laboratory of Marine Environmental Science, College of Oceanography and Environmental Science, Xiamen University, Xiamen, 361005 Fujian, China.
    Zhang, Yanjiao
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Rimphanitchayakit, Vichien
    Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
    Tassanakajon, Anchalee
    Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
    Andersson, M. Gunnar
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, The Linnaeus Centre for Bioinformatics.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    High sequence variability among hemocyte-specific Kazal-type proteinase inhibitors in decapod crustaceans2010In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 34, no 1, p. 69-75Article in journal (Refereed)
    Abstract [en]

    Crustacean hemocytes were found to produce a large number of transcripts coding for Kazal-type proteinase inhibitors (KPIs). A detailed study performed with the crayfish Pacifastacus leniusculus and the shrimp Penaeus monodon revealed the presence of at least 26 and 20 different Kazal domains from the hemocyte KPIs, respectively. Comparisons with KPIs from other taxa indicate that the sequences of these domains evolve rapidly. A few conserved positions, e.g. six invariant cysteines were present in all domain sequences whereas the position of P1 amino acid, a determinant for substrate specificity, varied highly. A study with a single crayfish animal suggested that even at the individual level considerable sequence variability among hemocyte KPIs produced exist. Expression analysis of four crayfish KPI transcripts in hematopoietic tissue cells and different hemocyte types suggest that some of these KPIs are likely to be involved in hematopoiesis or hemocyte release as they were produced in particular hemocyte types or maturation stages only.

  • 12.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Kawabata, Shun-ichiro
    Lee, Bok Luel
    Nonaka, Masaru
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Proteolytic cascades and their involvement in invertebrate immunity2010In: TIBS -Trends in Biochemical Sciences. Regular ed., ISSN 0968-0004, E-ISSN 1362-4326, Vol. 35, no 10, p. 575-583Article, review/survey (Refereed)
    Abstract [en]

    Bacteria and other potential pathogens are cleared rapidly from the body fluids of invertebrates by the immediate response of the innate immune system. Proteolytic cascades, following their initiation by pattern recognition proteins, control several such reactions, notably coagulation, melanisation, activation of the Toll receptor and complement-like reactions. However, there is considerable variation among invertebrates and these cascades, although widespread, are not present in all phyla. In recent years, significant progress has been made in identifying and characterizing these cascades in insects. Notably, recent work has identified several connections and shared principles among the different pathways, suggesting that cross-talk between them may be common.

  • 13.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Laurent, P
    Edsman, L
    Protection of natives in a plague situation.2002In: Bulletin Francais de la Peche et de la Pisciculture, ISSN 0767-2861, Vol. 367, p. 909-910Article in journal (Refereed)
  • 14.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lee, Bok Luel
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    The proPO-system: pros and cons for its role in invertebrate immunity2008In: Trends in immunology, ISSN 1471-4906, E-ISSN 1471-4981, Vol. 29, no 6, p. 263-271Article, review/survey (Refereed)
    Abstract [en]

    Melanisation is an important immune response in many invertebrates. Recent evidence also strongly implies that the melanisation (prophenoloxidase activating) cascade is intimately associated with the appearance of factors stimulating cellular defence by aiding phagocytosis and encapsulation reactions. However, some controversy exists in the field, and at least in flies and mosquitoes, the successful combat of some pathogens does not seem to be dependent on phenoloxidase activity. This may be because of redundancy among separate immune mechanisms, inappropriate testing, species differences or a combination thereof. Recently, by using RNA interference against phenoloxidase or in specific host-pathogen interactions where the pathogen prevents melanin production by the host, convincing data have confirmed the importance of this cascade in invertebrate innate immunity.

  • 15.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Coagulation in invertebrates2011In: Journal of Innate Immunity, ISSN 1662-811X, Vol. 3, no 1, p. 3-8Article, review/survey (Refereed)
    Abstract [en]

    In most animals there is a need to quickly prevent the loss of blood or equivalent fluids through inflicted injuries. In invertebrates with an open circulatory system (and sometimes a hydroskeleton as well) these losses may otherwise soon be fatal. Also, there is a need to prevent microbes that have gained access to the body through the wound from disseminating throughout the open circulatory system. Therefore, many invertebrates possess a coagulation system to prevent such accidents from having too serious consequences. In this review we discuss recent developments in a few animals - mainly arthropods - where more detailed data are available. It is likely, however, that corresponding systems are present in most phyla, but this is still unchartered territory.

  • 16.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Commentary: variable immune molecules in invertebrates2013In: Journal of Experimental Biology, ISSN 0022-0949, E-ISSN 1477-9145, Vol. 216, no 23, p. 4313-4319Article in journal (Other academic)
    Abstract [en]

    Recently it has become evident that invertebrates may mount a highly variable immune response that is dependent on which pathogen is involved. The molecular mechanisms behind this diversity are beginning to be unravelled and in several invertebrate taxa immune proteins exhibiting a broad range of diversity have been found. In some cases, evidence has been gathered suggesting that this molecular diversity translates into the ability of an affected invertebrate to mount a defence that is specifically aimed at a particular pathogen.

  • 17.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Crayfish immunity: Recent findings2018In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 80, p. 94-98Article in journal (Refereed)
    Abstract [en]

    Freshwater crayfish is an important commodity as well as a successful model for studies on crustacean immunity. Due to the ease with which they are kept and the available methods for hemocyte separation and culture they have proven to be very useful. Here, recent progress regarding pattern recognition, immune effector production and antiviral mechanisms are discussed. Several cases of functional resemblance between vertebrate complement and the crayfish immune reactions are highlighted.

  • 18.
    Cerenius, Lage
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Crustacean immune responses and their implications for disease control2012In: Infectious disease in aquaculture: prevention and control / [ed] Austin, B., Cambridge: Woodhead Publishing Limited, 2012, p. 69-87Chapter in book (Refereed)
    Abstract [en]

    This chapter reviews recent advances in our knowledge of crustacean immunity. Emphasis is given to shrimp due to their importance in aquaculture and trade and to freshwater crayfish since they serve as model organisms for research in crustacean immunology. Crustaceans lack antibodies, interferon and some other components from the mammalian immune arsenal but can still mount an efficient defence against many potential pathogens. Crustacean innate immunity relies on a combination of efficient hemocyte and humoral reactions carried out by plasma proteins.

  • 19.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    CRUSTACEAN IMMUNITY AND COMPLEMENT - A PREMATURE COMPARISON1995In: American Zoologist, ISSN 0003-1569, E-ISSN 2162-4445, Vol. 35, no 1, p. 60-67Article in journal (Refereed)
    Abstract [en]

    The prophenoloxidase activating system constitutes a system for recognition of foreignness in several invertebrates. The system has been especially well studied in crustaceans and it will now be possible to begin structural comparisons between components

  • 20.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Isolation of pattern recognition molecules from crustaceans1995In: Techniques in Fish Immunology 4, 155-160, 1995Chapter in book (Refereed)
  • 21.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Saprolegniaceae; zoospore formation, virulence and pathogenesis in animal hosts.1996In: Biology of lower fungi, 1996, p. 97-116Chapter in book (Refereed)
  • 22.
    Cerenius, Lage
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    The prophenoloxidase-activating system in invertebrates.2004In: Immunol Rev, ISSN 0105-2896, Vol. 198, p. 116-26Article in journal (Refereed)
  • 23. Dieguez-Uribeondo, Javier
    et al.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    The inhibition of extracellular proteinases from Aphanomyces spp by three different proteinase inhibitors from crayfish blood1998In: Mycological Research, ISSN 0953-7562, E-ISSN 1469-8102, Vol. 102, no 7, p. 820-824Article in journal (Refereed)
    Abstract [en]

    Three different proteinase inhibitors purified from crayfish blood, a 23 kDa inhibitor of subtilisin, a 155 kDa trypsin-inhibitor (pacifastin) and an alpha(2)-macroglobulin were tested for their inhibitory activities against extracellular proteinases from

  • 24. Dieguez-Uribeondo, Javier
    et al.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Dykova, I.
    Gelder, S.R.
    Hentonen, P.
    Jiravanichpaisal, Pikul
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lom, J.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Pathogens, parasites and ectocommensals.2006In: Atlas of crayfish in Europe: Distribution and Diseases., Publications Scientifiques du Muséum National d'Histoire Naturelle Vol. 64 “Patrimoines Naturels” , 2006, p. 135-155Chapter in book (Other (popular science, discussion, etc.))
  • 25.
    Diéguez-Uribeondo, Javier
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Evolutionary Biology, Physiological Botany.
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Evolutionary Biology, Physiological Botany.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Evolutionary Biology, Physiological Botany.
    Physiological characterization of Saprolegnia parasitica isolates from brown trout1996In: Aquaculture, ISSN 0044-8486, E-ISSN 1873-5622, Vol. 140, no 3, p. 247-257Article in journal (Refereed)
    Abstract [en]

    Saprolegnia parasitica has caused large mortalities in brown trout, Salmo trutta, in Spain. Several strains of Saprolegnia parasitica have been isolated from these epizootics and characterized regarding their physiological adaptation and genetic diversity

  • 26. Diéguez-Uribeondo, Javier
    et al.
    Fregeneda-Grandes, Juan M.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Pérez-Iniesta, Elena
    Aller-Gancedo, José Miguel
    Tellería, M. Teresa
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Martin, María P.
    Re-evaluation of the enigmatic species complex Saprolegnia diclina-Saprolegnia parasitica based on morphological, physiological and molecular data2007In: Fungal Genetics and Biology, ISSN 1087-1845, E-ISSN 1096-0937, Vol. 44, no 7, p. 585-601Article in journal (Refereed)
    Abstract [en]

    The phylogenetic relationships among isolates of the Saprolegnia diclina-Saprolegnia parasitica complex were investigated based on ITS rDNA sequences, and correlated with morphological and physiological characters. The isolates studied belong to five phylogenetically separate clades. The majority of presumed parasitic isolates, mostly isolated from fish lesions, fell within a clade that comprises isolates which has been variously named as S. diclina Type 1, S. parasitica, Saprolegnia salmonis or just as unnamed Saprolegnia sp. Presence of bundles of long-hooked hairs on secondary cysts, high frequency of retracted germination, and oogonia production at 7 degrees C (when occurring) were characteristic of this clade. A single isolate identified as S. diclina Type 2 clustered in a clade along with Saprolegnia ferax isolates. The isolates identified as S. diclina s. str. (S. diclina Type 3) distributed in two clades and appeared closely related to Saprolegnia multispora and to a number of Chilean isolates identified as Saprolegnia australis. The ITS sequences of clade I were almost identical even though the isolates were of diverse geographical origins and showed physiological and morphological differences and variations in their pathogenicity. This suggest these species reproduces clonally even in apparently sexually competent isolates. Adaptation to parasitism in Saprolegnia might have occurred at spore level by the development of long-hooked hairs to facilitate host attachment and selection of a retracting germination. The use of the name S. parasitica should be assigned to isolates of clade I that contained isolates forming cysts with bundles of long-hooked hairs.

  • 27. Diéguez-Uribeondo, Javier
    et al.
    García, Miguel A
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Kozubíková, Eva
    Ballesteros, Isabel
    Windels, Carol
    Weiland, John
    Kator, Howard
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Martín, María P
    Phylogenetic relationships among plant and animal parasites, and saprotrophs in Aphanomyces (Oomycetes)2009In: Fungal Genetics and Biology, ISSN 1087-1845, E-ISSN 1096-0937, Vol. 46, no 5, p. 365-376Article in journal (Refereed)
    Abstract [en]

    Molecular phylogenetic relationships among 12 species of Aphanomyces de Bary (Oomycetes) were analyzed based on 108 ITS sequences of nuclear rDNA. Sequences used in the analyses belonged to the major species currently available in pure culture and GenBank. Bayesian, maximum likelihood, and maximum parsimony analyses support that Aphanomyces constitutes a monophyletic group. Three independent lineages were found: (i) plant parasitic, (ii) animal parasitic, and (iii) saprotrophic or opportunistic parasitic. Sexual reproduction appeared to be critical in plant parasites for survival in soil environments while asexual reproduction seemed to be advantageous for exploiting specialization in animal parasitism. Repeated zoospore emergence seems to be an advantageous property for both plant and animal parasitic modes of life. Growth in unspecific media was generally faster in saprotrophs compared with parasitic species. A number of strains and GenBank sequences were found to be misidentified. It was confirmed molecularly that Aphanomyces piscicida and Aphanomyces invadans appear to be conspecific, and found that Aphanomyces iridis and Aphanomyces euteiches are closely related, if not the same, species. This study has shown a clear evolutionary separation between Aphanomyces species that are plant parasites and those that parasitize animals. Saprotrophic or opportunistic species formed a separate evolutionary lineage except Aphanomyces stellatus whose evolutionary position has not yet been resolved.

  • 28.
    Diéguez-Uribeondo, Javier
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Huang, TS
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Physiological adaptation of an Aphanomyces astaci strain isolated from the freshwater crayfish Procambarus clarkii 1995In: Mycological Research, ISSN 0953-7562, E-ISSN 1469-8102, Vol. 99, no 5, p. 574-578Article in journal (Refereed)
    Abstract [en]

    Physiological, epidemiological and genetical properties of an Aphanomyces astaci strain (Pc) isolated from the warm water crayfish, Procambarus clarkii, were compared to other A. astaci strains isolated from the cold water crayfish Astacus astacus,

  • 29.
    Donpudsa, Suchao
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Rimphanitchayakit, Vichien
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology.
    Tassanakajon, Anchalee
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Proteinase inhibitory activities of two two-domain Kazal proteinase inhibitors from the freshwater crayfish Pacifastacus leniusculus and the importance of the P2 position in proteinase inhibitory activity2010In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 29, no 5, p. 716-723Article in journal (Refereed)
    Abstract [en]

    Serine proteinase inhibitors are found ubiquitously in living organisms and involved in homeostasis of processes using proteinases as well as innate immune defense. Two two-domain Kazal-type serine proteinase inhibitors (KPIs), KPI2 and KPI8, have been identified from the hemocyte cDNA library of the crayfish Pacifastacus leniusculus. Unlike other KPIs from P. leniusculus, they are found specific to the hernocytes and contain an uncommon P-2 amino acid residue, Gly. To unveil their inhibitory activities, the two KPIs and their domains were over-expressed. By testing against subtilisin, trypsin, chymotrypsin and elastase, the KPI2 was found to inhibit strongly against subtilisin and weakly against trypsin, while the KPI8 was strongly active against only trypsin. With their P-1 Set and Lys residues, the KPI2_domain2 and KPI8_domain2 were responsible for strong inhibition against subtilisin and trypsin, respectively. Mutagenesis of KPI8_domain1 at P-2 amino acid residue from Gly to Pro, mimicking the P-2 residue of KPI8_domain2, rendered the KPI8_domain1 strongly active against trypsin, indicating the important role of P-2 residue in inhibitory activities of the Kazal-type serine proteinase inhibitors. Only the KPI2 was found to inhibit against the extracellular serine proteinases from the pathogenic oomycete of the freshwater crayfish, Aphanomyces astaci.

  • 30. Hernandez-Cortes, Patricia
    et al.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Garcia-Carreno, F
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Trypsin from Pacifastacus leniusculus hepatopancreas: Purification and cDNA cloning of the synthesized zymogen1999In: Biological chemistry (Print), ISSN 1431-6730, E-ISSN 1437-4315, Vol. 380, no 4, p. 499-501Article in journal (Refereed)
    Abstract [en]

    Trypsin was purified from crayfish, Pacifastacus leniusculus, hepatopancreas, and the gene that encoded this enzyme was cloned from a hepatopancreas cDNA library. Crayfish trypsin is synthesized as a zymogen according to the sequence of the putative precu

  • 31.
    Huang, TS
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Wang, HY
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lee, SY
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Johansson, MW
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade2000In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 275, no 14, p. 9996-10001Article in journal (Refereed)
    Abstract [en]

    A cDNA encoding a protein resembling masquerade, a serine proteinase homologue expressed during embryogenesis, larval, and pupal development in Drosophila melanogaster, was identified in hemocytes of the adult freshwater crayfish, Pacifastacus leniusculus. The crayfish protein is similar to Drosophila masquerade in the following aspects: (a) overall sequence of the serine proteinase domain, such as the position of three putative disulfide bridges, glycine in the place of the catalytic serine residue, and the presence of a substrate-lining pocket typical for trypsins; (b) the presence of several copies of a disulfide-knotted motif in the putative propeptide. This masquerade-like protein is cleaved into a 27-kDa fragment, which could be detected by immunoblot analysis using an affinity-purified antibody against a synthetic peptide in the C-terminal domain of the protein. The 27-kDa protein could be immunoaffinity-purified from hemocyte lysate supernatant and exhibited cell adhesion activity in vitro, indicating that the C-terminal domain of the crayfish masquerade-like protein mediates cell adhesion.

  • 32.
    Johansson, Karin C
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Cerenius, Lage
    Diptericin expression in bacteria infected Drosophila mbn-2 cells - effect of infection dose and phagocytosisManuscript (Other (popular science, discussion, etc.))
  • 33.
    Johansson, Karin C
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Diptericin expression in bacteria infected Drosophila mbn-2 cells - effect of infection dose and phagocytosis.2006In: Insect molecular biology (Print), ISSN 0962-1075, E-ISSN 1365-2583, Vol. 15, no 1, p. 57-62Article in journal (Refereed)
    Abstract [en]

    Drosophila haemocytes play a key role in defence against microbial aggression. Their capacity to sense and dispose of bacteria and also to signal to other immune tissues is probably vital to overcome an infection. In this work we used the haemocyte-like mbn-2 cell line to investigate how expression of the antimicrobial peptide diptericin is affected after a high dose bacterial challenge with diaminopimelic acid (DAP)-peptidoglycan Gram-positive and Gram-negative bacteria. We report that diptericin expression is negatively affected by high infection dose and rapid bacterial growth regardless of the type of infection and bacterial virulence and occurs in the absence of mbn-2 cell death. Furthermore we show that the mbn-2 cell population is heterogeneous, containing both phagocytic and nonphagocytic cells and that contact with large numbers of bacteria decreases diptericin expression in the phagocytic cell population.

  • 34. Lilley, J H
    et al.
    Hart, D
    Panyawachira, V
    Kanchanakhan, S
    Chinabut, S
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Molecular characterization of the fish-pathogenic fungus Aphanomyces invadans.2003In: Journal of Fish Diseases, ISSN 0140-7775, E-ISSN 1365-2761, Vol. 26, no 5, p. 263-75Article in journal (Refereed)
    Abstract [en]

    Aphanomyces invadans (Saprolegniaceae) is a peronosporomycete fungus associated with the serious fish disease, epizootic ulcerative syndrome (EUS), also known as mycotic granulomatosis. In this study, interspecific relationships were examined between A. invadans isolates and other aquatic animal pathogenic Saprolegniaceae, and saprophytic Saprolegniaceae from EUS-affected areas. Restriction fragment length polymorphisms and sequences of ribosomal DNA confirmed that A. invadans is distinct from all other species studied. A sequence from the internal transcribed spacer region ITS1, unique to A. invadans, was used to design primers for a PCR-based diagnostic test. Intraspecific relationships were also examined by random amplification of polymorphic DNA using 20 isolates of A. invadans from six countries. The isolates showed a high degree of genetic homogeneity using 14 random ten-mer primers. This provides evidence that the fungus has spread across Asia in one relatively rapid episode, which is consistent with reports of outbreaks of EUS. Physiological distinctions between A. invadans and other Aphanomyces species based on a data set of 16 growth parameters showed remarkable taxonomic congruence with the molecular phylogeny.

  • 35. Lilley, JH
    et al.
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    RAPD evidence for the origin of crayfish plague outbreaks in Britain1997In: Aquaculture, ISSN 0044-8486, E-ISSN 1873-5622, Vol. 157, no 3-4, p. 181-185Article in journal (Refereed)
    Abstract [en]

     

    Two isolates of Aphanomyces astaci obtained from diseased white-clawed crayfish (Austropotamobius pallipes) in Herefordshire, England were compared against representative isolates of three groups of the fungus found in Sweden and one from Spain by means of random amplification of polymorphic DNA (RAPD). The English isolates proved to be very similar to a Swedish strain which is considered to have been introduced from North America with shipments of the signal crayfish (Pacifastacus leniusculus) from 1970 onwards, and has since spread to indigenous populations of noble crayfish (Astacus astacus). This strain has not been found to be involved in recent incidences of crayfish plague in Turkey and Spain. It is therefore most likely that at least some of the outbreaks of crayfish plague in England resulted from imports of P. leniusculus from northern Europe after 1970, or directly from North America.

  • 36. Lilley, J.H.
    et al.
    Hart, D.
    Panayawachira, V.
    Kanachanakhan, S.
    Chinabut, K.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
    Molecular characterisation of the fish-pathogenic fungus Aphanomyces invadans2003In: Journal of Fish Diseases, Vol. 26, no 5, p. 263-275Article in journal (Refereed)
    Abstract [en]

    Aphanomyces invadans (Saprolegniaceae) is a peronosporomycete fungusassociated with the serious fish disease, epizootic ulcerative syndrome ( EUS), also known as mycotic granulomatosis. In this study, interspecific relationships were examined between A. invadans isolates and other aquatic animal pathogenic Saprolegniaceae, and saprophytic Saprolegniaceae from EUS-affected areas. Restriction fragment length polymorphisms and sequences of ribosomal DNA confirmed that A. invadans is distinct from all other species studied. A sequence from the internal transcribed spacer region ITS1, unique to A. invadans, was used to design primers for a PCR-based diagnostic test. Intraspecific relationships were also examined by random amplification of polymorphic DNA using 20 isolates of A. invadans from six countries. The isolates showed a high degree of genetic homogeneity using 14 random ten-mer primers. This provides evidence that the fungus has spread across Asia in one relatively rapid episode, which is consistent with reports of outbreaks of EUS. Physiological distinctions between A. invadans and otherAphanomyces species based on a data set of 16 growth parameters showed remarkable taxonomic congruence with the molecular phylogeny.

  • 37. Lilley, JH
    et al.
    Hart, D
    Richards, RH
    Roberts, RJ
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Pan-Asian spread of single fungal clone results in large scale fish kills1997In: The Veterinary Record, ISSN 0042-4900, E-ISSN 2042-7670, Vol. 140, no 25, p. 653-654Article in journal (Refereed)
  • 38.
    Lin, Xionghui
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Lee, B.L.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Purification of properoxinectin, a myeloperoxidase homologue and its activation to a cell adhesion molecule2007In: Biochimica et Biophysica Acta - General Subjects, ISSN 0304-4165, E-ISSN 1872-8006, Vol. 1770, no 1, p. 87-93Article in journal (Refereed)
    Abstract [en]

    Peroxidases are important mediators of innate immune reactions throughout the animal kingdom. In many arthropods a myeloperoxidase homologue, peroxinectin, is known to function as a cell adhesion factor and an opsonin. Here, we report in the freshwater crayfish Pacifastacus leniusculus the isolation of properoxinectin, inactive in cell adhesion, and we also show that properoxinectin is produced in the mature blood cells whereas the hematopoietic tissue contains very little of this protein. Both properoxinectin and peroxinectin are catalytically active as peroxidases, at least when using low molecular weight substrates. The extracellular processing of properoxinectin into an active cell adhesion protein was found to involve proteolytic steps shared with the prophenoloxidase activating system to yield catalytically active phenoloxidase. Thus, the regulation of activities by two ancient metalloproteins, both potentially producing highly toxic substances aimed at pathogens, is carried out by limited proteolysis. The proteolytic processing is triggered in the presence of microbial compounds such as beta-glucans or lipopolysaccharide after the release of properoxinectin and prophenoloxidase activating serine proteinases from the blood cells.

  • 39.
    Liu, Haipeng
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Jiravanichpaisal, Pikul
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Bok, Luel Lee
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Phenoloxidase is an important component of the defense against Aeromonas hydrophila infection in a crustacean, Pacifastacus leniusculus2007In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 282, no 46, p. 33593-33598Article in journal (Refereed)
    Abstract [en]

    The melanization cascade, in which phenoloxidase is the terminal enzyme, appears to play a key role in recognition of and defense against microbial infections in invertebrates. Here, we show that phenoloxidase activity and melanization are important for the immune defense toward a highly pathogenic bacterium, Aeromonas hydrophila, in the freshwater crayfish, Pacifastacus leniusculus. RNA interference-mediated depletion of crayfish prophenoloxidase leads to increased bacterial growth, lower phagocytosis, lower phenoloxidase activity, lower nodule formation, and higher mortality when infected with this bacterium. In contrast, if RNA interference of pacifastin, an inhibitor of the crayfish prophenoloxidase activation cascade, is performed, it results in lower bacterial growth, increased phagocytosis, increased nodule formation, higher phenoloxidase activity, and delayed mortality. Our data therefore suggest that phenoloxidase is required in crayfish defense against an infection by A. hydrophila, a highly virulent and pathogenic bacterium to crayfish.

  • 40.
    Liu, Haipeng
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Jiravanichpaisal, Pikul
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Irene
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus2006In: Journal of Virology, ISSN 0022-538X, E-ISSN 1098-5514, Vol. 80, no 21, p. 10365-10371Article in journal (Refereed)
    Abstract [en]

    In a study of genes expressed differentially in the freshwater crayfish Pacifastacus leniusculus infected experimentally with the white spot syndrome virus (WSSV), one protein, known as antilipopolysaccharide factor (ALF), was chosen, among those whose transcript levels increased upon viral infection, for further studies. ALF RNA interference (RNAi) experiments in whole animals and in cell cultures indicated that ALF can protect against WSSV infection, since knockdown of AILF by RNAi specifically resulted in higher rates of viral propagation. In a cell culture of hematopoietic tissue (Hpt) from P. leniusculus, quantitative PCR showed that knockdown of ALF by RNAi resulted into WSSV levels that were about 10-fold higher than those treated with control double-stranded RNA (dsRNA). In addition, RNAi experiments with other crayfish genes that had been found to be up-regulated by a WSSV infection did not result in any changes of viral loads. Thus, the cell culture does not respond to dsRNA in a similar manner, as shown earlier for dsRNA injected into shrimp, which gave a higher degree of resistance to WSSV infection. If ALF transcription in whole animals was stimulated by the administration of LTV-treated WSSV, a partial protection against a subsequent challenge with the active virus was conferred to the host. This is the first crustacean gene product identified with the capacity to interfere with replication of this important pathogen.

  • 41. Oidtmann, B
    et al.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Schmid, I
    Hoffmann, R
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Crayfish plague epizootics in Germany - classification of two German isolates of the crayfish plague fungus Aphanomyces astaci by random amplification of polymorphic DNA1999In: Diseases of Aquatic Organisms, ISSN 0177-5103, E-ISSN 1616-1580, Vol. 35, no 3, p. 235-238Article in journal (Refereed)
    Abstract [en]

    Following 2 outbreaks of crayfish plague in southern Germany, the causative agent, the oomycete fungus Aphanomyces astaci, was isolated from the diseased Astacus astacus. The identity of the 2 strains was confirmed using established techniques, such as ph

  • 42. Oidtmann, B
    et al.
    Schaefers, N
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Hoffmann, R W
    Detection of genomic DNA of the crayfish plague fungus Aphanomyces astaci (Oomycete) in clinical samples by PCR.2004In: Veterinary Microbiology, ISSN 0378-1135, E-ISSN 1873-2542, Vol. 100, no 3-4, p. 269-82Article in journal (Refereed)
    Abstract [en]

    A diagnostic procedure, based on a polymerase chain reaction method (PCR) was developed to detect infection of crayfish with the Oomycete Aphanomyces astaci. A set of oligonucleotide primers was designed to specifically amplify A. astaci DNA in the ITS region surrounding the 5.8S rDNA gene. The PCR amplifies a 115 bp amplicon. The specificity of the primers was demonstrated by testing on 27 A. astaci strains and against 20 non-A. astaci Oomycetes and 5 fungal species. Most of the non-A. astaci Oomycete or fungal species included in the study are either known parasites of freshwater crayfish cuticle or can be found in their natural environment. Specificity was also tested against crayfish tissue and some known parasites and bacteria infecting crayfish.A protocol for the extraction of A. astaci DNA from infected crayfish tissue was developed. The optimised method allows the detection of two genome equivalents of purified A. astaci genomic DNA.The method was tested on noble crayfish (Astacus astacus), artificially infected with A. astaci. Detection of A. astaci was possible at the very first time of sampling, which was 2 days after the beginning of spore exposure

  • 43. Ragan, MA
    et al.
    Goggin, CL
    Cawthorn, RJ
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Jamieson, AVC
    Plourde, SM
    Rand, TG
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Gutell, RR
    A novel clade of protistan parasites near the animal-fungal divergence1996In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 93, no 21, p. 11907-11912Article in journal (Refereed)
    Abstract [en]

    Sequences of nuclear-encoded small-subunit rRNA genes have been determined for representatives of the enigmatic genera Dermocystidium, Ichthyophonus, and Psorospermium, protistan parasites of fish and crustaceans. The small-subunit rRNA genes from these p

  • 44.
    Royo, Felix
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Andersson, Gunnar
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Bangyeekhun, Eakaphun
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. Jämförande fysiologi.
    Mazquiz, Jose Luis
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Söderhäll, Kenneth
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Cerenius, Lage
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology. jämförande fysiologi.
    Physiological and genetic characterisation of some new Aphanomyces strains isolated from freshwater crayfish.2004In: Vet Microbiol, ISSN 0378-1135, Vol. 104, no 1-2, p. 103-12Article in journal (Refereed)
  • 45.
    Sritunyalucksana, Kallaya
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon1999In: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 23, no 3, p. 179-186Article in journal (Refereed)
    Abstract [en]

     

    A cDNA encoding shrimp, Penaeus monodon, prophenoloxidase (proPO) was obtained by screening a hemocyte library by plaque hybridization using a proPO cDNA fragment from freshwater crayfish, Pacifastacus leniusculus, as a probe. The 3,002 bp cDNA contains an open reading frame of 2,121 bp and a 881 bp 3′-untranslated region. The molecular mass of the deduced amino acid sequence (688 amino acids) is 78,700 Da with an estimated pI of 5.8. Two putative copper binding sites are present and they have a highly conserved sequence around these sites. No signal peptide was detected in the shrimp proPO, as has been previously shown to be the case for all arthropod proPOs cloned so far. The cleavage site of zymogen activation is likely to be between Arg 44 and Val 45. A tentative complement-like motif (GCGWPQHM) is also present. Shrimp proPO mRNA is synthesized in the hemocytes and not in the hepatopancreas. Comparison of amino acid sequences showed that shrimp proPO is more closely related to another crustacean proPO, namely crayfish, than to the insect proPOs.

  • 46.
    Söderhäll, Kenneth
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Role of the prophenoloxidase-activating system in invertebrate immunity1998In: Current Opinion in Immunology, ISSN 0952-7915, E-ISSN 1879-0372, Vol. 10, no 1, p. 23-28Article in journal (Refereed)
    Abstract [en]

    The melanization reaction, which is a common response to parasite entry in invertebrate animals, especially arthropods, is due to the activity of an oxidoreductase, phenoloxidase. This enzyme is part of a complex system of proteinases, pattern recognition

  • 47. Vennerström, Pia
    et al.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    The origin of two crayfish plague (Aphanomyces astaci) epizootics in Finland on noble crayfish, Astacus astacus1998In: Annales Zoologici Fennici, ISSN 0003-455X, E-ISSN 1797-2450, Vol. 35, no 1, p. 43-46Article in journal (Refereed)
    Abstract [en]

    A fungus identified as Aphanomyces astaci was isolated from two crayfish plague epizootics among noble crayfish, Astacus astacus, in Central Finland. The isolated fungal strains from Vaikkojoki, Kaavi and Iso-Suojarvi, Saarijarvi were able to kill healthy

  • 48. Wang, RG
    et al.
    Lee, SY
    Cerenius, Lage
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Söderhäll, Kenneth
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
    Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus2001In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 268, no 4, p. 895-902Article in journal (Refereed)
    Abstract [en]

    The prophenoloxidase activating enzyme (ppA), a serine proteinase catalyzing the conversion of prophenoloxidase to an active phenoloxidase, has a molecular mass of about 36 kDa in its active form. This protein was cloned from a blood cell cDNA library and its corresponding cDNA of 1736 base pairs encodes a zymogenic protein (proppA) of 468 amino acids. An antibody raised against a synthetic peptide derived from a region of the cDNA sequence could efficiently inhibit the β-1,3-glucan triggered activation of prophenoloxidase in vitro. The C-terminal half of the proppA is composed of a typical serine proteinase domain, with a sequence similar to other invertebrate and vertebrate serine proteinases. The N-terminal half contains a cationic glycine-rich domain, a cationic proline-rich domain and a clip-domain, in which the disulfide-bonding pattern is likely to be identical to those of the horseshoe crab big defensin and mammalian β-defensins. Antibodies made against both the C- and the N-terminal halves recognize two proppAs under reducing conditions. However, under nonreducing conditions only the anti-C antibody recognized the two proppAs, which suggests that a conformational change takes place upon reduction that allows the anti-N to react with the N-terminal half of proppA. The recombinant clip-domain in crayfish proppA was overexpressed in Escherichia coli and the resulting peptide exhibited antibacterial activity against Gram-positive bacterial strains such as Micrococcus luteus Ml11 and Bacillus megaterium Bm11 with 50% growth inhibitory concentrations of 1.43 µm and 17.9 µm, respectively. These results suggest that the clip-domains in proppAs may function as antibacterial peptides.

1 - 48 of 48
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