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The role of cationic amino acid residues in the lethal activity of stonustoxin from stonefish (Synanceja horridat) venom
Author(s) -
Khoo HoonEng,
Chen Desong,
Yuen Raymond
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201682
Subject(s) - succinylation , lysine , venom , cytolysis , arginine , cationic polymerization , biochemistry , amino acid , chemistry , protein subunit , biology , cytotoxicity , in vitro , organic chemistry , gene
Stonustoxin (SNTX) is a two subunit pore‐forming cytolytic protein purified from the venom of the stonefish (Synanceja horrida). SNTX also possesses lethal activity. Since cationic residues contribute significantly to the cytolytic activity of several pore‐forming toxins, we examined the role of lysine and arginine residues in the lethal activity of SNTX. SNTX lost its lethal activity when the positively‐charged side chains of lysine residues were converted to negatively‐charged side chains upon succinylation. When the arginine residues were modified using 2,3‐butanedione, SNTX also lost its lethal activity. However, the domains for cytolytic and lethal activity may not necessarily be the same.