Chicken lung lectin is a functional C-type lectin and inhibits haemagglutination by influenza A virus

Many proteins of the calcium-dependent (C-type) lectin family have been shown to play an important role in innate immunity. They can bind to a broad range of carbohydrates, which enables them to interact with ligands present on the surface of micro-organisms. We previously reported the finding of a...

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Bibliographic Details
Published in:Veterinary microbiology 2008-07, Vol.130 (1), p.37-46
Main Authors: Hogenkamp, Astrid, Isohadouten, Najiha, Reemers, Sylvia S.N., Romijn, Roland A., Hemrika, Wieger, White, Mitchell R., Tefsen, Boris, Vervelde, Lonneke, van Eijk, Martin, Veldhuizen, Edwin J.A., Haagsman, Henk P.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
animal proteins
Animals
binding properties
biochemical mechanisms
Biological and medical sciences
C-type lectin
carbohydrate binding
Chicken lung lectin
chickens
Chickens - metabolism
disease resistance
Female
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
hemagglutination
Hemagglutination, Viral - drug effects
hemagglutinins
immune response
immunity
in vitro studies
Influenza A virus
Influenza A virus - physiology
inhibitors
Innate immunity
lectins
Lectins - metabolism
Lectins - pharmacology
Lung - metabolism
lungs
mannose
Microbiology
Miscellaneous
neutralization
Neutralization Tests
Protein Structure, Tertiary
Recombinant Proteins
Virology
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Summary:Many proteins of the calcium-dependent (C-type) lectin family have been shown to play an important role in innate immunity. They can bind to a broad range of carbohydrates, which enables them to interact with ligands present on the surface of micro-organisms. We previously reported the finding of a new putative chicken lectin, which was predominantly localized to the respiratory tract, and thus termed chicken lung lectin (cLL). In order to investigate the biochemical and biophysical properties of cLL, the recombinant protein was expressed, affinity purified and characterized. Recombinant cLL was expressed as four differently sized peptides, which is most likely due to post-translational modification. Crosslinking of the protein led to the formation of two high-molecular weight products, indicating that cLL forms trimeric and possibly even multimeric subunits. cLL was shown to have lectin activity, preferentially binding to α-mannose in a calcium-dependent manner. Furthermore, cLL was shown to inhibit the haemagglutination-activity of human isolates of influenza A virus, subtype H3N2 and H1N1. These result show that cLL is a true C-type lectin with a very distinct sugar specificity, and that this chicken lectin could play an important role in innate immunity.
ISSN:0378-1135
1873-2542
DOI:10.1016/j.vetmic.2007.12.008