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An MBL-like protein may interfere with the activation of the proPO-system, an important innate immune reaction in invertebrates
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Organismal Biology, Comparative Physiology.
Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University.
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2013 (English)In: Immunobiology, ISSN 0171-2985, E-ISSN 1878-3279, Vol. 218, no 2, 159-168 p.Article in journal (Refereed) Published
Abstract [en]

An important characteristic of the innate immune systems of crayfish and other arthropods is the activation of a serine proteinase cascade in the hemolymph, which results in the activation of prophenoloxidase and subsequently leading to the formation of toxic quinones and melanin. Although no true complement homologues have been detected in crayfish or crustaceans, several proteins with similarities to vertebrate pattern recognition receptors (PRRs), which are involved in the lectin pathway of complement activation in vertebrates, are present. One is a C-type lectin, a mannose-binding lectin (Pl-MBL), which is secreted from granular hemocytes. Here we report that Pl-MBL has LPS-binding capacity and is dependent upon high Ca(2+) for its solubility and Pl-MBL interferes with proPO activation in vitro when HLS is prepared at high Ca(2+). The proPO-activating system is efficiently activated by microbial polysaccharides and it has to be neatly regulated to avoid activation in places where it is inappropriate and the active enzyme PO should be prevented from spreading throughout the body of the animal. This may be particularly important during molting when proPO is involved in hardening of a new cuticle and the animal is vulnerable to microbes. The presence of high amount of Pl-MBL in the granular hemocytes may play a role in this process. Since a hemocyte lysate supernatant (HLS) prepared at 100mM Ca(2+) could become activated when the concentration of LPS was increased up to 3mg/ml, this may indicate that Pl-MBL acts as a scavenger for LPS to prevent spreading of LPS in the hemolymph to avoid further activation of the proPO-system.

Place, publisher, year, edition, pages
2013. Vol. 218, no 2, 159-168 p.
Keyword [en]
C-type lectin, Mannose-binding lectin (MBL), LPS, Pacifastacus leniusculus, proPO-system
National Category
Immunology
Identifiers
URN: urn:nbn:se:uu:diva-173685DOI: 10.1016/j.imbio.2012.02.011ISI: 000315312000004PubMedID: 22459272OAI: oai:DiVA.org:uu-173685DiVA: diva2:524584
Note

De 2 första författarna delar förstaförfattarskapet.

Available from: 2012-05-03 Created: 2012-05-03 Last updated: 2017-12-07Bibliographically approved

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Söderhäll, IreneSöderhäll, Kenneth

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