Cloning And Functional Analysis Of Grass Carp Collagen Lectin Gene
Keywords
C-Type Lectin, Collagen Lectin, Glycosyl Recognition Domain, Expression, Grass Carp
Abstract
The collagen lectin gene was cloned from the liver and kidney cdna library of grass carp (ctenopharyngodonidella). The full-length cdna of grass carp collagen lectin is 1128 bp, including 229 bp in the 5? untranslated region, 104 bp in the 3? untranslated region, and a maximum open reading frame of 795 bp, encoding 264 amino acids. Phylogenetic analysis showed that grass carp collagen lectin has the closest genetic relationship with zebrafish. According to the sequence characteristics of grass carp collagen lectin, the cDNA containing the glycosyl recognition domain (crd) was cloned, and its recombinant protein PCRD was obtained by prokaryotic expression and purification. The agglutination and sugar inhibition experiments between PCRD and 6 kinds of bacteria were carried out. The results showed that the four sugars of galactose, glucose, mannose and maltose would significantly reduce the agglutination of PCRD and Aeromonas hydrophila and even greatly interfere with the agglutination; maltose made gold The agglutination of Staphylococcus aureus is significantly reduced, while peptidoglycan and mannose inhibit aggregation; in addition, the agglutination reaction of PCRD does not depend on Ca2+.
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Original research was done by Li Qin, Ma Meisheng, Hu Chengyu
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