Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/22213
Title: Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae.
Authors: Gilbert, RJ
Rossjohn, J
Parker, MW
Tweten, RK
Morgan, PJ
Mitchell, TJ
Errington, N
Rowe, AJ
Andrew, PW
Byron, O
First Published: 11-Dec-1998
Citation: J MOL BIOL, 1998, 284 (4), pp. 1223-1237
Abstract: The pathogenically important cholesterol-binding pore-forming bacterial "thiol-activated" toxins (TATs) are commonly believed to be monomeric in solution and to undergo a transition on membrane binding mediated by cholesterol to an oligomeric pore. We present evidence, gained through the application of a number of biochemical and biophysical techniques with associated modelling, that the TAT from Streptococcus pneumoniae, pneumolysin, is in fact able to self-associate in solution to form the same oligomeric structures. The weak interaction leading to solution oligomerization is manifested at low concentrations in a dimeric toxin form. The inhibition of toxin self-interaction by derivatization of the single cysteine residue in pneumolysin with the thiol-active agent dithio (bis)nitrobenzoic acid indicates that self-interaction is mediated by the fourth domain of the protein, which has a fold similar to other proteins known to self-associate. This interaction is thought to have implications for the understanding of mechanisms of pore formation and complement activation by pneumolysin.
DOI Link: 10.1006/jmbi.1998.2258
ISSN: 0022-2836
Links: http://hdl.handle.net/2381/22213
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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