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Titolo:
The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins
Autore:
Shepard, LA; Shatursky, O; Johnson, AE; Tweten, RK;
Indirizzi:
Univ Oklahoma, Hlth Sci Ctr, Dept Microbiol & Immunol, Oklahoma City, OK 73190 USA Univ Oklahoma Oklahoma City OK USA 73190 nol, Oklahoma City, OK 73190 USA Texas A&M Univ, Dept Med Biochem & Genet, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 Genet, College Stn, TX 77843 USA Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 t Chem, College Stn, TX 77843 USA Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 iophys, College Stn, TX 77843 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 33, volume: 39, anno: 2000,
pagine: 10284 - 10293
SICI:
0006-2960(20000822)39:33<10284:TMOPAF>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
STAPHYLOCOCCAL ALPHA-TOXIN; STREPTOLYSIN-O; ERYTHROCYTE-MEMBRANES; PROTECTIVE ANTIGEN; PERFRINGOLYSIN-O; FORMING TOXINS; FLUORESCENCE; AEROLYSIN; CHANNELS; OLIGOMERIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Tweten, RK Univ Oklahoma, Hlth Sci Ctr, Dept Microbiol & Immunol, 940 Stanton L YoungBlvd,BMSB,Room 1053, Oklahoma City, OK 73190 USA Univ Oklahoma 940 Stanton L Young Blvd,BMSB,Room 1053 Oklahoma City OK USA 73190
Citazione:
L.A. Shepard et al., "The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins", BIOCHEM, 39(33), 2000, pp. 10284-10293

Abstract

Perfringolysin O (PFO) is a member of the cholesterol-dependent cytolysin (CDC) family of membrane-penetrating toxins. The CDCs form large homooligomers (estimated to be comprised of up to 50 CDC monomers) that are responsible for generating a large pore in cholesterol-containing membranes of eukaryotic cells. The assembly of the PFO cytolytic complex was examined to determine whether it forms an oligomeric prepore complex on the membrane prior to the insertion of its membrane-spanning beta-sheet. A PFO oligomeric complex was formed on liposomes at both 4 degrees C and 37 degrees C and shown by SDS-agarose gel electrophoresis to be comprised of a large, comparatively homogeneous complex instead of a distribution of oligomer sizes. At low temperature, the processes of oligomerization and membrane insertion could be resolved, and PFO was found to form an oligomer without significant membrane insertion of its beta-hairpins. Furthermore, PFO was found to increase the ion conductivity through a planar bilayer by large and discrete stepwise changes in conductance that are consistent with the insertion of a preassembled pore complex into the bilayer. The combined results of these analyses strongly support the hypothesis that PFO forms a large oligomeric preporecomplex on the membrane surface prior to the insertion of its transmembrane beta-sheet.

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Documento generato il 30/03/20 alle ore 09:47:32