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Crossing three membranes Channel formation by aerolysin
Author(s) -
Buckley J.Thomas
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80896-o
Subject(s) - aerolysin , membrane , biophysics , channel (broadcasting) , chemistry , computer science , biology , biochemistry , computer network , virulence , gene
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 formation.