TY - JOUR
T1 - Anthrax toxin
T2 - channel-forming activity of protective antigen in planar phospholipid bilayers
AU - Blaustein, R. O.
AU - Koehler, T. M.
AU - Collier, R. J.
AU - Finkelstein, A.
PY - 1989
Y1 - 1989
N2 - The three separate proteins that make up anthrax toxin - protective antigen (PA), edema factor (EF), and lethal factor (LF) - act in binary combinations to produce two distinct reactions in experimental animals: edema (PA + EF) and death (PA + LF). PA is believed to interact with a membrane receptor, and after proteolytic processing, to mediate endocytosis and subsequent translocation of EF or LF into the cytosol. PA can be separated, after mild trypsinolysis, into two fragments, PA65 (65 kDa) and PA20 (20 kDa). We demonstrate that trypsin-cleaved PA is capable of forming cation-selective channels in planar phospholipid bilayer membranes and that this activity is confined to the PA65 fragment; PA20, LF, and EF are devoid of channel-forming activity. These PA65 channels exhibit pH-dependent and voltage-dependent activity - a property reminiscent of the channels formed by the two-chain proteins diphtheria, tetanus, and botulinum toxins.
AB - The three separate proteins that make up anthrax toxin - protective antigen (PA), edema factor (EF), and lethal factor (LF) - act in binary combinations to produce two distinct reactions in experimental animals: edema (PA + EF) and death (PA + LF). PA is believed to interact with a membrane receptor, and after proteolytic processing, to mediate endocytosis and subsequent translocation of EF or LF into the cytosol. PA can be separated, after mild trypsinolysis, into two fragments, PA65 (65 kDa) and PA20 (20 kDa). We demonstrate that trypsin-cleaved PA is capable of forming cation-selective channels in planar phospholipid bilayer membranes and that this activity is confined to the PA65 fragment; PA20, LF, and EF are devoid of channel-forming activity. These PA65 channels exhibit pH-dependent and voltage-dependent activity - a property reminiscent of the channels formed by the two-chain proteins diphtheria, tetanus, and botulinum toxins.
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U2 - 10.1073/pnas.86.7.2209
DO - 10.1073/pnas.86.7.2209
M3 - Article
C2 - 2467303
AN - SCOPUS:0024523836
SN - 0027-8424
VL - 86
SP - 2209
EP - 2213
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 7
ER -