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Evolutionary conservation of mannan-binding lectin (MBL) in bony fish

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Authors:
  • Kania, Per Walther ;
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    Department of Cancer and Inflammation Research, Department of Molecular Medicine, Faculty of Health Sciences, University of Southern Denmark
  • Sorensen, Rasmus Reng ;
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    unknown
  • Koch, Claus ;
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    Department of Cancer and Inflammation Research, Department of Molecular Medicine, Faculty of Health Sciences, University of Southern Denmark
  • Brandt, Jette ;
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    Faculty of Health Sciences, University of Southern Denmark
  • Kliem, Anette ;
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    Faculty of Health Sciences, University of Southern Denmark
  • Vitved, Lars ;
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    Department of Cancer and Inflammation Research, Department of Molecular Medicine, Faculty of Health Sciences, University of Southern Denmark
  • Hansen, Søren ;
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    Orcid logo0000-0002-8186-4630
    Department of Cancer and Inflammation Research, Department of Molecular Medicine, Faculty of Health Sciences, University of Southern Denmark
  • Skjødt, Karsten
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    Department of Cancer and Inflammation Research, Department of Molecular Medicine, Faculty of Health Sciences, University of Southern Denmark
Subtitle:
identification, characterization and expression analysis of three bona fide collectin homologues of MBL in the rainbow trout (Onchorhynchus mykiss)
DOI:
10.1016/j.fsi.2010.07.020
Abstract:
The complement system of fish is generally as complex as in mammals, and in addition Teleost fish often possess several genes encoding different subtypes of a given complement component, such as C3-1, C3-3 and C3-4. Initiators of both the classical (C1) and alternative pathway (factor B) have been characterized in the rainbow trout but so far no molecules of the lectin pathway have been identified. Based on the generally accepted idea of complement evolution, which predicts that the alternative pathway predates the two other pathways, and that the lectin pathway developed before the classical, we set out to characterize members of the lectin pathway in fish. We identified and characterized three homologues of mannan-binding lectin (MBL) with a bona fide collectin structure. By means of RT-PCR and immunohistochemistry using monoclonal antibodies we found that they were synthesized in the spleen, the anterior intestine and the liver. In the liver, we saw co-expression with mannan-binding lectin associated serine protease (MASP). The MBL homologues 2 and 3 (MBL-H2,3) were also found in the vascular system of the rainbow trout. By means of gel size exclusion chromatography of serum we found that MBL-H2,3 oligomerized heterogeneously from monomers to tetramers of a trimeric collagenous subunit. Sequence comparison and phylogenetic studies showed that the homologues were more related with MBL than any other collectins, and that two previously characterized trout proteins, designated MBL1 and MBL2, should be reconsidered as MBL candidates.
Type:
Journal article
Language:
English
Published in:
Fish and Shellfish Immunology, 2010, Vol 29, Issue 6, p. 910-20
Keywords:
Mannan-binding lectin (MBL); Mannan-binding lectin associated serine protease (MASP); Collectin; Complement; Innate immunity; Former LIFE faculty
Main Research Area:
Medical science
Publication Status:
Published
Review type:
Peer Review
Submission year:
2010
Scientific Level:
Scientific
ID:
112178348

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