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. 1998 Mar;44(3):643-6.
doi: 10.1080/15216549800201682.

The role of cationic amino acid residues in the lethal activity of stonustoxin from stonefish (Synanceja horrida) venom

H E Khoo  1 , D Chen, R Yuen
Affiliations

The role of cationic amino acid residues in the lethal activity of stonustoxin from stonefish (Synanceja horrida) venom

H E Khoo et al. Biochem Mol Biol Int. 1998 Mar.

Abstract

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.

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