Molecular Cloning and
Sequence Analysis of cDNA Encoding Acutolysin C, a Hemorrhagic
Metalloproteinase, from Agkistrodon acutus
LIU Qing-Du, XU Wei-Hua, CHENG Xin, LIU Jing*
( School of Life Science, University of Science and Technology of China,
Hefei 230027, China )
Abstract A
full-length cDNA of 1 650 bp was amplified from the snake venom gland cDNA
library of Agkistrodon acutus. Analysis of the nucleotide sequence
indicated that the amplified cDNA contained a complete open reading frame
encoding 417 amino acid residues including signal peptide sequence, zymogen
sequence and proteinase domain. The zymogen sequence contained CGVT motif that
was highly conserved in almost all venom metalloproteinases. The
metalloproteinase domain contained a conserved signature zinc-binding motif
HEXXHXXGXXH in the catalytic region and the CIM turn. It shares high similarity
with the sequence of acutolysin C deduced from crystallographic data, and with
other class P-I snake venom hemorrhagic toxins.
Key words Agkistrodon acutus； hemorrhagic metalloproteinase； cDNA cloning； crystallographic sequence
*Corresponding author： Tel, 86-551-3606294； Fax, 86-551-3601441； e-mail： [email protected]