Buckley J T
Department of Biochemistry and Microbiology, University of Victoria, B.C., Canada.
FEBS Lett. 1992 Jul 27;307(1):30-3. doi: 10.1016/0014-5793(92)80896-o.
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 oligomer is 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 formation.
