title: Chicken lung lectin is a functional C-type lectin and inhibits haemagglutination by influenza A virus.
abstract: 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 alpha-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.
authors.affiliation: Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.175, 3508 TD Utrecht, The Netherlands.
authors.forename: Astrid
authors.initials: A
authors.lastname: Hogenkamp
authors.forename: Najiha
authors.initials: N
authors.lastname: Isohadouten
authors.forename: Sylvia S N
authors.initials: SS
authors.lastname: Reemers
authors.forename: Roland A
authors.initials: RA
authors.lastname: Romijn
authors.forename: Wieger
authors.initials: W
authors.lastname: Hemrika
authors.forename: Mitchell R
authors.initials: MR
authors.lastname: White
authors.forename: Boris
authors.initials: B
authors.lastname: Tefsen
authors.forename: Lonneke
authors.initials: L
authors.lastname: Vervelde
authors.forename: Martin
authors.initials: M
authors.lastname: van Eijk
authors.forename: Edwin J A
authors.initials: EJ
authors.lastname: Veldhuizen
authors.forename: Henk P
authors.initials: HP
authors.lastname: Haagsman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens / Q000378:metabolism*; D005260:Female; D005786:Gene Expression Regulation; D006387:Hemagglutination, Viral / Q000187:drug effects*; D009980:Influenza A virus / Q000502:physiology*; D037102:Lectins / Q000378:metabolism* / Q000494:pharmacology; D008168:Lung / Q000378:metabolism*; D009500:Neutralization Tests; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins
chemical_list: D037102:Lectins; D011994:Recombinant Proteins