TY - JOUR
T1 - Channels formed in phospholipid bilayer membranes by diphtheria, tetanus, botulinum and anthrax toxin
AU - Finkelstein, A.
PY - 1990
Y1 - 1990
N2 - Diphtheria, tetanus, botulinum, and anthrax toxin are multipartate toxins, one of the domains of which is (or is presumed to be) an enzyme. Cell intoxication requires that the enzymatic portion gain access to the cytosol via endocytosis into an acidic vesicle compartment of the cell. Translocation of the enzyme across the vesicular membrane is dependent on the low pH of the vesicle and involves another domain of the toxin; for each of these toxins, that domain is capable of forming channels in phospholipid bilayer membranes. These channels are large (> 12 Å diameter) and voltage-gated, and the pH conditions required for their formation in lipid bilayers are similar to those existing in acidic vesicles and required for cell intoxication.
AB - Diphtheria, tetanus, botulinum, and anthrax toxin are multipartate toxins, one of the domains of which is (or is presumed to be) an enzyme. Cell intoxication requires that the enzymatic portion gain access to the cytosol via endocytosis into an acidic vesicle compartment of the cell. Translocation of the enzyme across the vesicular membrane is dependent on the low pH of the vesicle and involves another domain of the toxin; for each of these toxins, that domain is capable of forming channels in phospholipid bilayer membranes. These channels are large (> 12 Å diameter) and voltage-gated, and the pH conditions required for their formation in lipid bilayers are similar to those existing in acidic vesicles and required for cell intoxication.
KW - acidic pH
KW - channel gating
KW - protein translocation
KW - voltage dependence
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M3 - Article
C2 - 1705290
AN - SCOPUS:0025053196
SN - 0021-7948
VL - 84
SP - 188
EP - 190
JO - Journal de Physiologie
JF - Journal de Physiologie
IS - 2
ER -