Gilbert, R. J.C., Rossjohn, J., Parker, M. W., Tweten, R. K., Morgan, P. J., Mitchell, T. J., Errington, N., Rowe, A. J., Andrew, P. W. and Byron, O. (1998) Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae. Journal of Molecular Biology, 284(4), pp. 1223-1237. (doi: 10.1006/jmbi.1998.2258) (PMID:9837740)
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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.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Byron, Professor Olwyn |
Authors: | Gilbert, R. J.C., Rossjohn, J., Parker, M. W., Tweten, R. K., Morgan, P. J., Mitchell, T. J., Errington, N., Rowe, A. J., Andrew, P. W., and Byron, O. |
College/School: | College of Medical Veterinary and Life Sciences > School of Life Sciences |
Journal Name: | Journal of Molecular Biology |
Publisher: | Academic Press |
ISSN: | 0022-2836 |
ISSN (Online): | 1089-8638 |
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