Key result
Trp-433->Phe pneumolysin mutation cuts haemolysis by ~95% versus wild-type and forms cation-insensitive channels.
Why the study?
The role of the conserved Trp-Glu-Trp-Trp sequence in pneumolysin channel formation and function after membrane binding and oligomerization was unclear.
The Trp-433 residue in pneumolysin is critical for functional channel formation subsequent to cell membrane binding and oligomerization.
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Trp-433 mutation impairs pneumolysin channel function; leaves open its targeting in pneumococcal cardiovascular complications.
KORCHEV et al. (1998) studied this question. Pneumolysin mutation Trp-433-->Phe vs. Wild-type pneumolysin was evaluated on Haemolysis or leakage of low-molecular-mass metabolites. The pneumolysin mutation Trp-433-->Phe resulted in less than 5% of wild-type haemolysis or leakage and formed large channels insensitive to cation-induced closure.
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