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Angthong, P., Roytrakul, S., Jarayabhand, P. & Jiravanichpaisal, P. (2017). Characterization and function of a tachylectin 5-like immune molecule in Penaeus monodon. Developmental and Comparative Immunology, 76, 120-131
Öppna denna publikation i ny flik eller fönster >>Characterization and function of a tachylectin 5-like immune molecule in Penaeus monodon
2017 (Engelska)Ingår i: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 76, s. 120-131Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Tachylectin5A and its homolog, tachylectin5B both contain a fibrinogen-related domain (FReD) and have been studied in horseshoe crabs, Tachypleus tridentatus and Carcinoscorpius rotundicauda and shown to be involved in host defense. Here, we demonstrate the presence of tachylectin5-like genes in shrimp, Penaeus monodon, designated as Penlectin5-1 (PL5-1) and Penlectin5-2 (PL5-2), which both contain a signal peptide and a single FReD with an acetyl group and a calcium binding sites and they are both structurally similar to horseshoe crab tachylectin/carcinolectin5. The PL5-land PL5-2 transcript were expressed in various shrimp tissues in normal shrimp, and their expression was upregulated in tissues such as hemocytes and hindgut following challenge with pathogenic Vibrio harveyi. The PL5-2 protein was detected in various tissues as well as in cell-free hemolymph. The biological function of the PL5-2 protein is to recognize some Gram-positive and Gram-negative bacteria regardless whether they are non-pathogenic or pathogenic. They have hemagglutination activity on human erythrocyte and bacterial agglutination activity to both Gram negative and Gram positive bacteria. Possible binding sites of PL5-2 to bacteria could be at the N-acetyl moiety of the G1cNAc-MurNAc cell wall of the peptidoglycan since the binding could be inhibited by G1cNAc or GaINAC. The presence of PL5-2 protein in both circulating hemolymph and intestine, where host and microbes are usually interacting, may suggest that the physiological function of shrimp tachylectin-like proteins is to recognize and bind to invading bacteria to immobilize and entrap these microbes and subsequently clear them from circulation and the host body, and probably to control and maintain the normal flora in the intestine.

Ort, förlag, år, upplaga, sidor
ELSEVIER SCI LTD, 2017
Nyckelord
Tachylectin, Lectin, Fibrinogen-related domain, Innate immunity
Nationell ämneskategori
Immunologi Zoologi
Identifikatorer
urn:nbn:se:uu:diva-330524 (URN)10.1016/j.dci.2017.05.023 (DOI)000407985100013 ()28587859 (PubMedID)
Tillgänglig från: 2017-10-09 Skapad: 2017-10-09 Senast uppdaterad: 2017-10-09
Angthong, P., Roytrakul, S., Jarayabhand, P. & Jiravanichpaisal, P. (2017). Involvement of a tachylectin-like gene and its protein in pathogenesis of acute hepatopancreatic necrosis disease (AHPND) in the shrimp, Penaeus monodon. Developmental and Comparative Immunology, 76, 229-237
Öppna denna publikation i ny flik eller fönster >>Involvement of a tachylectin-like gene and its protein in pathogenesis of acute hepatopancreatic necrosis disease (AHPND) in the shrimp, Penaeus monodon
2017 (Engelska)Ingår i: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 76, s. 229-237Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

A shrimp disease, the so-called acute hepatopancreatic necrosis disease (AHPND) is caused by a specific strain of Vibrio parahaemolyticus (VP) and it has resulted in significant losses to the global shrimp farming industry. In our previous study, three of tachylectin-like genes were cloned and characterized from the intestine of Penaeus monodon, designated as Penlectin5-1 (PL5-1), Penlectin5-2 (PL5-2) and Penlectin5-3 (PL5-3). These three genes all contain fibrinogen-related domain (FReD). The expression level of PL5-1, PL5-2 and PL5-3 was elevated in the stomach after oral administration with AHPND-causing V. parahaemolyticus 3HP (VP3HP). A polyclonal antibody to PL5-2 was successfully produced in a rabbit using the purified recombinant P15-2 as an immunogen, and this because only the predominant protein PL5-2 could be successfully purified from shrimp plasma by affinity chromatography using a N-Acetyl-oglucosamine column allowed us to perform functional studies of this lectin. The native purified PL5-2 protein had binding and agglutination activities towards VP3HR To further understand the functions and the involvements of this lectin in response to AHPND in shrimp, RNAi-mediated knockdown of PL5-1, PL5-2 or PL5-3 was performed prior to an oral administration of VP3HP. As a result, Penlectin5-silencing in shrimp challenged with VP3HP showed higher mortality and resulted in more severe histopathological changes in the hepatopancreas with typical signs of AHPND. These results therefore suggest a role for crustacean fibrinogen-related proteins (FRePs) in innate immune response during the development of AHPND, and maybe also during other infections.

Ort, förlag, år, upplaga, sidor
ELSEVIER SCI LTD, 2017
Nyckelord
Tachylectin, Lectin, EMS/AHPND, Innate immunity
Nationell ämneskategori
Immunologi Zoologi
Identifikatorer
urn:nbn:se:uu:diva-330526 (URN)10.1016/j.dci.2017.06.011 (DOI)000407985100024 ()28655576 (PubMedID)
Tillgänglig från: 2017-10-09 Skapad: 2017-10-09 Senast uppdaterad: 2017-10-09
Wu, C., Noonin, C., Jiravanichpaisal, P., Söderhäll, I. & Söderhäll, K. (2012). An insect TEP in a crustacean is specific for cuticular tissues and involved in intestinal defense. Insect Biochemistry and Molecular Biology, 42(2), 71-80
Öppna denna publikation i ny flik eller fönster >>An insect TEP in a crustacean is specific for cuticular tissues and involved in intestinal defense
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2012 (Engelska)Ingår i: Insect Biochemistry and Molecular Biology, ISSN 0965-1748, E-ISSN 1879-0240, Vol. 42, nr 2, s. 71-80Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

In an attempt to identify genes encoding thioester-containing proteins in the freshwater crayfish, Pacifastacus leniusculus, three different cDNAs were found. A phylogenetic analysis of these proteins indicates that they can be classified into two subfamilies: two alpha-2-macroglobulins (Pl-A2M1, Pl-A2M2) showing a close similarity to shrimp A2M, and one insect TEP-like protein (Pl-TEP). This is the first report of an insect TEP-like protein in a crustacean. Crayfish Pl-A2M1, Pl-A2M2 and Pl-TEP cDNAs encode proteins with 1480, 1586 or 1507 amino acids, respectively. Pl-A2M1, Pl-A2M2 and Pl-TEP have the basic domain structure and functionally important residues for each molecule, and their mRNA was detected in different parts of the body, suggesting that they may have different functions. Pl-A2M1 was mainly expressed in hemocytes and Pl-A2M2 was highly expressed in heart and nerve, while Pl-TEP was exclusively expressed in cuticular tissues such as gill and intestine. RNA interference of Pl-TEP in vivo resulted in that these animals were slightly less resistant when fed with the bacterium, Pseudomonas libanensis/gessardii. Furthermore, when TEP activity was blocked using methylamine followed by bacterial feeding, the animals were killed to a higher extent compared to a control group. Taken together, this indicates that Pl-TEP and/or Pl-A2M1, Pl-A2M2 may be important for the immune defense in crayfish intestine and function as a pattern recognition protein in crayfish cuticular tissues.

Nationell ämneskategori
Immunologi
Forskningsämne
Biologi med inriktning mot jämförande fysiologi
Identifikatorer
urn:nbn:se:uu:diva-165581 (URN)10.1016/j.ibmb.2011.10.006 (DOI)000300271500001 ()22193393 (PubMedID)
Tillgänglig från: 2012-01-09 Skapad: 2012-01-09 Senast uppdaterad: 2017-12-08Bibliografiskt granskad
Söderhäll, K., Watthanasurorot, A., Söderhäll, I. & Jiravanichpaisal, P. (2012). DSCAM (Down syndrome adhesion molecule); structure and function in a crustacean.. In: : . Paper presented at The 12th Congress of the International Society of Developmental and Comparative Immunology,Hilton Fukuoka Sea Hawk Hotel, Fukuoka city, Japan,9th to 13th July, 2012..
Öppna denna publikation i ny flik eller fönster >>DSCAM (Down syndrome adhesion molecule); structure and function in a crustacean.
2012 (Engelska)Konferensbidrag, Enbart muntlig presentation (Övrigt vetenskapligt)
Abstract [en]

In invertebrates, the circulating blood cells (hemocytes) are crucial for protecting the animal against invading microorganisms, and they are directly involved in recognition, phagocytosis, melanization and cytotoxic reactions. Many microorganisms trigger hemocyte synthesis and release from the HPT, and this may be one way for the host to respond to an infection. Therefore we have studied hematopoiesis intensely and have now in detail deciphered the molecular mechanisms in hematopoietic stem cell proliferation and differentiation. Recently we have cloned Dscam proteins from P. leniusculus. The Down syndrome cell adhesion molecule (Dscam) is a member of the immunoglobulin super family of proteins. In vertebrates Dscam was first identified for its importance in developing neural tissue, and for its critical role in Down Syndrome.These cell adhesion molecules are large proteins containing ten Ig domains and six fibronectin type III domains, and this structure is conserved across animal phyla. There are two Dscam genes in humans (DSCAM), and there are evidences for a conserved essential role in neural wiring, in both vertebrate and insects. An intriguing difference in Dscam gene structure is the exon duplication that have occurred in arthropods and which give rise to an array of alternative spliced isoforms in insects and crustaceans. Alternative splicing of individual exon sequences occurs in a mutually exclusive manner and allows for expression of several thousands of isoforms.

We have now shown that hemocytes that express different spliced isoforms are induced by specific challenge, and moreover that these specific forms are important in clearing bacteria. This differential splicing may be one new area of research that may help to explain how crustaceans and insects as effectively can manage to distinguish between harmless and harmful microorganisms.

Nationell ämneskategori
Immunologi
Identifikatorer
urn:nbn:se:uu:diva-189808 (URN)
Konferens
The 12th Congress of the International Society of Developmental and Comparative Immunology,Hilton Fukuoka Sea Hawk Hotel, Fukuoka city, Japan,9th to 13th July, 2012.
Tillgänglig från: 2013-01-04 Skapad: 2013-01-04 Senast uppdaterad: 2016-11-03
Söderhäll, I., Söderhäll, K., Noonin, C., Jiravanichpaisal, P. & Wu, C. (2012). TEPs (thioester containing proteins) and ficolins: structure and function in a crustacean. Paper presented at The 12th Congress of the International Society of Developmental and Comparative Immunology,Hilton Fukuoka Sea Hawk Hotel, Fukuoka city, Japan, 9th to 13th July, 2012..
Öppna denna publikation i ny flik eller fönster >>TEPs (thioester containing proteins) and ficolins: structure and function in a crustacean
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2012 (Engelska)Konferensbidrag, Poster (med eller utan abstract) (Övrigt vetenskapligt)
Nationell ämneskategori
Immunologi
Identifikatorer
urn:nbn:se:uu:diva-189811 (URN)
Konferens
The 12th Congress of the International Society of Developmental and Comparative Immunology,Hilton Fukuoka Sea Hawk Hotel, Fukuoka city, Japan, 9th to 13th July, 2012.
Anmärkning

This is the first report of an insect TEP-like protein in a crustacean. Pl-TEPs have the basic domain structure and functionally important residues ,and their mRNA was detected in different parts of the body, suggesting that they may have different functions. Pl-A2M1 was mainly expressed in hemocytes and Pl-A2M2 was highly expressed in heart and nerve, while Pl-TEP was exclusively expressed in cuticular tissues such as gill and intestine. RNA interference of Pl-TEP in vivo resulted in that these animals were slightly less resistant when fed with the bacterium, Pseudomonas libanensis/gessardii. Furthermore, when TEP activity was blocked using methylamine followed by bacterial feeding, the animals were killed to a higher extent compared to a control group. Taken together, this indicates that Pl-TEP and/or Pl-A2M1, Pl-A2M2 may be important for the immune defense in crayfish intestine and function as a pattern recognition protein in cray␣sh cuticular tissues.

To isolate pathogen-associated molecular patterns (PAMPs)-binding molecules, the bacter- ium, Staphylococcus aureus was used as an affinity matrix to find bacteria-binding proteins in the plasma of the freshwater crayfish, Pacifastacus leniusculus. Two new bacteria-binding ficolin-like proteins (FLPs) were identified by 2-DE and MS analysis. The FLPs have a fibri- nogen-related domain (FReD) in their C-terminal and a repeat region in their N-terminal regions with putative structural similarities to the collagen-like domain of vertebrate ficolins and mannose binding lectins (MBLs).. Recombinant FLPs exhibited agglutination activity of Gram-negative bacteria Escherichia coli and Aeromonas hydrophila in the presence of Ca21. The FLPs could bind to A. hydrophila, E. coli as well as S. aureus as judged by bacteria adsorption. Moreover, the FLPs may help crayfish to clear Gram-negative bacteria, but not Gram-positive bacteria which had been injected into the hemolymph.

Tillgänglig från: 2013-01-04 Skapad: 2013-01-04 Senast uppdaterad: 2013-01-08Bibliografiskt granskad
Noonin, C., Jiravanichpaisal, P., Söderhäll, I., Merino, S., Tomás, J. M. & Söderhäll, K. (2010). Melanization and Pathogenicity in the Insect, Tenebrio molitor, and the Crustacean, Pacifastacus leniusculus, by Aeromonas hydrophila AH-3. PLoS ONE, 5(12), e15728
Öppna denna publikation i ny flik eller fönster >>Melanization and Pathogenicity in the Insect, Tenebrio molitor, and the Crustacean, Pacifastacus leniusculus, by Aeromonas hydrophila AH-3
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2010 (Engelska)Ingår i: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 5, nr 12, s. e15728-Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Aeromonas hydrophila is the most common Aeromonas species causing infections in human and other animals such as amphibians, reptiles, fish and crustaceans. Pathogenesis of Aeromonas species have been reported to be associated with virulence factors such as lipopolysaccharides (LPS), bacterial toxins, bacterial secretion systems, flagella, and other surface molecules. Several mutant strains of A. hydrophila AH-3 were initially used to study their virulence in two animal species, Pacifastacus leniusculus (crayfish) and Tenebrio molitor larvae (mealworm). The AH-3 strains used in this study have mutations in genes involving the synthesis of flagella, LPS structures, secretion systems, and some other factors, which have been reported to be involved in A. hydrophila pathogenicity. Our study shows that the LPS (O-antigen and external core) is the most determinant A. hydrophila AH-3 virulence factor in both animals. Furthermore, we studied the immune responses of these hosts to infection of virulent or non-virulent strains of A. hydrophila AH-3. The AH-3 wild type (WT) containing the complete LPS core is highly virulent and this bacterium strongly stimulated the prophenoloxidase activating system resulting in melanization in both crayfish and mealworm. In contrast, the ΔwaaE mutant which has LPS without O-antigen and external core was non-virulent and lost ability to stimulate this system and melanization in these two animals. The high phenoloxidase activity found in WT infected crayfish appears to result from a low expression of pacifastin, a prophenoloxidase activating enzyme inhibitor, and this gene expression was not changed in the ΔwaaE mutant infected animal and consequently phenoloxidase activity was not altered as compared to non-infected animals. Therefore we show that the virulence factors of A. hydrophila are the same regardless whether an insect or a crustacean is infected and the O-antigen and external core is essential for activation of the proPO system and as virulence factors for this bacterium.

Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
urn:nbn:se:uu:diva-141552 (URN)10.1371/journal.pone.0015728 (DOI)000285793200045 ()21206752 (PubMedID)
Tillgänglig från: 2011-01-12 Skapad: 2011-01-12 Senast uppdaterad: 2017-12-11
Jiravanichpaisal, P., Lee, S.-Y., Kim, Y.-A., Andrén, T. & Söderhäll, I. (2007). Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: Characterization and expression pattern. Developmental and Comparative Immunology, 31(5), 441-455
Öppna denna publikation i ny flik eller fönster >>Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: Characterization and expression pattern
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2007 (Engelska)Ingår i: Developmental and Comparative Immunology, ISSN 0145-305X, E-ISSN 1879-0089, Vol. 31, nr 5, s. 441-455Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

A 14 amino acid residues proline/arginine-rich antibacterial peptide designated as astacidin 2 was purified and characterized from hemocytes of the freshwater crayfish, Pacifastacus leniusculus. Astacidin 2 has a broad range of antibacterial activity against both Gram-positive and Gram-negative bacteria. The primary sequence of astacidin 2 is RPRPNYRPRPIYRP with an amidated C-terminal and the molecular mass is 1838 Da determined by mass spectrometry. Furthermore, the cDNA of three different crustin antibacterial homologs were isolated from a crayfish hemocyte EST library. RT-PCR was used to analyze the expression of the genes coding for astacidin 2 and P. leniusculus crustins (Plcrustin) 1–3 after bacterial challenge. The expression of Plcrustin1 was upregulated in both hemocytes and hematopoietic tissue after challenge with Gram-negative Escherichia coli or Acinetobacter ssp. non pathogenic bacteria as well as by a Gram negative crayfish pathogenic bacterium (Aeromonas hydrophila). The PlCrustin3 transcript was only upregulated after inoculation with the non-pathogenic Acinetobacter ssp. while there was no change in expression of Plcrustin2 or astacidin 2 following a bacterial challenge.

Nyckelord
Antibacterial protein, Proline-rich peptide, Astacidin 2, Crustin, Carcinin, Crayfish, Pacifastacus leniusculus, Innate immunity
Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
urn:nbn:se:uu:diva-19137 (URN)10.1016/j.dci.2006.08.002 (DOI)000244674500002 ()17049601 (PubMedID)
Tillgänglig från: 2008-05-15 Skapad: 2008-05-15 Senast uppdaterad: 2017-12-08Bibliografiskt granskad
Jiravanichpaisal, P., Puanglarp, N., Petkon, S., Donnuea, S., Söderhäll, I. & Söderhäll, K. (2007). Expression of immune-related genes in larval stages of the giant tiger shrimp, Penaeus monodon. Fish and Shellfish Immunology, 23(4), 815-824
Öppna denna publikation i ny flik eller fönster >>Expression of immune-related genes in larval stages of the giant tiger shrimp, Penaeus monodon
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2007 (Engelska)Ingår i: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 23, nr 4, s. 815-824Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Shrimp undergo several morphologically different stages during development and therefore the expression of some immune-related genes such as prophenoloxidase (proPO), peroxinectin (Prx), crustin (Crus), penaeidin (Pen), transglutaminase (TGase), haemocyanin (Hc) and astakine (Ak) were determined during larval development of the shrimp (Penaeus monodon), i.e. nauplius 4 (N4), protozoea 1 and 3 (Z1 and 3), mysis 3 (My 3), post-larvae 3 (PL3) and also in haemocytes of juveniles. Semi-quantitative RT-PCR analysis showed that all transcripts were already present in the early larval stage of N4 but at different levels. The transcript of proPO was found to be extremely low or even absent at N4, whereas Prx, Crus, Pen, TGase, Hc and Ak were significantly expressed at all larval stages. Up to now expression of proPO and Prx has only been reported from haemocytes in crustaceans and in this study Prx also appeared to be expressed in stages which appear to lack haemocytes. Thus, this may suggest that Prx is expressed in other cells than haemocytes. It is well known among invertebrates that the proPO system plays a crucial role as an immune effector molecule against microbes. However, in this study, the transcript of proPO was low during the larval stages and hardly present at all at N4. This might indicate that the development of immune-competent haemocytes during the larval stages is not completed and as a consequence they are likely to be more susceptible to infectious diseases during these stages.

Nyckelord
Shrimp larvae, Penaeus monodon, Prophenoloxidase, Peroxinectin, Transglutaminase
Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
urn:nbn:se:uu:diva-11713 (URN)10.1016/j.fsi.2007.03.003 (DOI)000249092800010 ()17490892 (PubMedID)
Tillgänglig från: 2007-10-15 Skapad: 2007-10-15 Senast uppdaterad: 2017-12-11
Liu, H., Jiravanichpaisal, P., Cerenius, L., Bok, L. L., Söderhäll, I. & Söderhäll, K. (2007). Phenoloxidase is an important component of the defense against Aeromonas hydrophila infection in a crustacean, Pacifastacus leniusculus. Journal of Biological Chemistry, 282(46), 33593-33598
Öppna denna publikation i ny flik eller fönster >>Phenoloxidase is an important component of the defense against Aeromonas hydrophila infection in a crustacean, Pacifastacus leniusculus
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2007 (Engelska)Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 282, nr 46, s. 33593-33598Artikel i tidskrift (Refereegranskat) Published
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.

Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
urn:nbn:se:uu:diva-97411 (URN)10.1074/jbc.M706113200 (DOI)000250840200040 ()17855335 (PubMedID)
Tillgänglig från: 2008-08-18 Skapad: 2008-08-18 Senast uppdaterad: 2017-12-14Bibliografiskt granskad
Liu, H., Jiravanichpaisal, P., Söderhäll, I., Cerenius, L. & Söderhäll, K. (2006). Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus. Journal of Virology, 80(21), 10365-10371
Öppna denna publikation i ny flik eller fönster >>Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus
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2006 (Engelska)Ingår i: Journal of Virology, ISSN 0022-538X, E-ISSN 1098-5514, Vol. 80, nr 21, s. 10365-10371Artikel i tidskrift (Refereegranskat) Published
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.

Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
urn:nbn:se:uu:diva-97410 (URN)10.1128/JVI.01101-06 (DOI)000241606100008 ()17041217 (PubMedID)
Tillgänglig från: 2008-08-18 Skapad: 2008-08-18 Senast uppdaterad: 2017-12-14Bibliografiskt granskad
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