Current Zoology(formerly Acta Zoologica Sinica),    2009, 55(5): 376 - 382
Title: Characterization of the cDNA encoding a BPI/LBP homologue in venom gland of the hundred-pace snake Deinagkistrodon acutus
Authors: Jianrao HU, Mingfu CAO, Jiong Chen
 C o l l e g e   o f   L i f e   a n d   E n v i r o n m e n t a l   S c i e n c e s ,   H a n g z h o u   N o r m a l   U n i v e r s i t y ,   H a n g z h o u   3 1 0 0 3 6 ,   C h i n a 
Abstract:
Bactericidal/permeability-increasing protein (BPI) and LPS-binding protein (LBP) play an important role in host defence. Current evidence shows that BPI/LBP may be widely existed in different cells and tissue types of animals. A full-length cDNA clone encoding a BPI/LBP homologue (dBPI), 1757bp in size, was characterized in venom gland of the hundred-pace snake Deinagkistrodon acutus. Its deduced amino acid sequence of 417 residues had 13.8%–21.5% identity to BPI like 1(BPIL1) and BPI like 3(BPIL3) of other animals. Conserved cysteine residues which are involved in disulfide bond formation between the final strand of the N-terminal beta sheet and the long alpha helix of BPI are identified as Cys146-Cys183 of dBPI. Phylogenetic tree analysis showed that the BPI/LBP homologues formed five large clusters and dBPI was in a large cluster including BPIL1 and BPIL3. dBPI mRNA shows a tissue specific expression in venom gland. This is the first study to identify the cDNA encoding BPI/LBP homologues from reptiles [Current Zoology 55 (5): 376–382, 2009].

Keywords: Hundred-pace snake, Venom gland, BPI/LBP homologue, Phylogeny, mRNA expression patterns

*Correspondence should be addressed to Jianrao HU (E-mail:hujianrao@126.com).

PDF [2856.0 KB]

 

This page has been browsed 5842 times. The paper has been downloaded 1524 times.