Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0300-9084(00)00203-0
Title: The role of tryptophan residues in the hemolytic activity of stonustoxin, a lethal factor from stonefish (Synanceja horrida) venom
Authors: Yew, W.S.
Khoo, H.E. 
Issue Date: 2000
Citation: Yew, W.S., Khoo, H.E. (2000). The role of tryptophan residues in the hemolytic activity of stonustoxin, a lethal factor from stonefish (Synanceja horrida) venom. Biochimie 82 (3) : 251-257. ScholarBank@NUS Repository. https://doi.org/10.1016/S0300-9084(00)00203-0
Abstract: Stonustoxin (SNTX) is a pore-forming cytolytic lethal factor, isolated from the venom of the stonefish Synanceja horrida, that has potent hemolytic activity. The role of tryptophan residues in the hemolytic activity of SNTX was investigated. Oxidation of tryptophan residues of SNTX with N-bromosuccinimide (NBS) resulted in loss of hemolytic activity. Binding of 8-anilino-1-naphthalenesulphonate (ANS) to SNTX resulted in occlusion of tryptophan residues that resulted in loss of hemolytic activity. Circular dichroism and fluorescence studies indicated that ANS binding resulted in a conformational change of SNTX, in particular, a relocation of surface tryptophan residues to the hydrophobic interior. NBS-modification resulted in oxidised surface tryptophan residues that did not relocate to the hydrophobic interior. These results suggest that native surface tryptophan residues play a pivotal role in the hemolytic activity of SNTX, possibly by being an essential component of a hydrophobic surface necessary for pore-formation. This study is the first report on the essentiality of tryptophan residues in the activity of a lytic and lethal factor from a fish venom. (C) 2000 Societe francaise de biochimie et biologie moleculaire / Editions scientifiques et medicales Elsevier SAS.
Source Title: Biochimie
URI: http://scholarbank.nus.edu.sg/handle/10635/38159
ISSN: 03009084
DOI: 10.1016/S0300-9084(00)00203-0
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