Cloning, expression and characterization of two C-type lectins from the venom gland of Bungarus multicinctus.
C-type lectins found in many animals are non-enzymatic proteins and able to bind with mono- and oligosaccharides in a Ca(2+)-dependent fashion. Here, we report the cloning of two C-type lectins named BML-1 and BML-2 from the venom gland of Bungarus multicinctus, and expression of their mature peptides with 135 and 137 amino acids as inclusion bodies. Recombinant BML-1 and BML-2 proteins with 135 amino acids formed monomers, and those with 137 amino acids formed homodimers and monomers and both of them displayed certain hemagglutinating activity to rabbit erythrocytes. The results of Western blotting and immuno-affinity chromatography demonstrated that C-type lectins in B. multicinctus formed dimers in physiological conditions, and their molecular weight is lower than previous predictions. This is the first report of the cloning of the BML-2 gene from the venom gland of B. multicinctus, as well as an investigation of its confirmation and biological functions.
Lin
Lu-Ping
LP
Key Laboratory of the Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Fujian 361005, China.
Lin
Qun
Q
Wang
Yi-Quan
YQ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017838:Bungarus / Q000235:genetics; D003001:Cloning, Molecular; D005786:Gene Expression Regulation; D037181:Lectins, C-Type / Q000737:chemistry* / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D012910:Snake Venoms / Q000737:chemistry* / Q000235:genetics
D037181:Lectins, C-Type; D012910:Snake Venoms