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  • Title: Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae.
    Author: Gilbert RJ, Rossjohn J, Parker MW, Tweten RK, Morgan PJ, Mitchell TJ, Errington N, Rowe AJ, Andrew PW, Byron O.
    Journal: J Mol Biol; 1998 Dec 11; 284(4):1223-37. PubMed ID: 9837740.
    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.
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