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 a-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.
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 a-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.
Original language | English |
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Pages (from-to) | 37-46 |
Number of pages | 10 |
Journal | Veterinary Microbiology |
Volume | 130 |
Publication status | Published - 2008 |
Keywords
- Chicken lung lectin
- Innate immunity
- Influenza A virus
- C-type lectin