Crossing three membranes Channel formation by aerolysin
- 27 July 1992
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 307 (1), 30-33
- https://doi.org/10.1016/0014-5793(92)80896-o
Abstract
Aerolysin is a channel-forming toxin responsible for the pathogenicity of Aeromonas hydrophila. It crosses the inner and outer membranes of the bacteria in separate steps and is released as a 52-kDa inactive protoxin which is activated by proteolytic removal of approximately 40 amino acids from the C terminus. The toxin binds to the erythrocyte transmembrane protein glycophorin and oligomerizes before inserting into the membrane, producing a voltage gated, anion selective channel about 1 nm in diameter. Remarkably, proaerolysin appears to be dimeric, whereas the oligomeris a heptamer. Using chemical modification and site-directed mutagenesis, we have identified some of the regions of the molecule which appear to be involved in secretion and in channel formationThis publication has 19 references indexed in Scilit:
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