Vibrio cholerae OmpU and OmpT porins are differentially affected by bile

被引:96
作者
Wibbenmeyer, JA
Provenzano, D
Landry, CF
Klose, KE
Delcour, AH
机构
[1] Univ Houston, Dept Biol & Biochem, Houston, TX 77204 USA
[2] Univ Texas, Hlth Sci Ctr, Dept Microbiol, San Antonio, TX 78229 USA
关键词
D O I
10.1128/IAI.70.1.121-126.2002
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
OmpT and OmpU are pore-forming proteins of the outer membrane of Vibrio cholerae, a pathogen that colonizes the intestine and produces cholera. Expression of the ompU and ompT genes is under the regulation of ToxR, a transmembrane transcriptional activator that also controls expression of virulence factors. It was recently shown that bile stimulates the ToxR-mediated transcription of ompU and that ompU-expressing strains are more resistant to bile and anionic detergents than ompT-expressing cells. In order to further understand the role of the OmpT and OmpU porins in the ability of V. cholerae to survive and colonize the host intestine, we examined the outer membrane permeability of cells expressing only ompU or only ompT or both genes in the absence and in the presence of bile. By comparing various strains in terms of the rate of degradation of the beta -lactam antibiotic cephaloridine by the periplasmic beta -lactamase, we found that the permeation of the antibiotic through the outer membrane of OmpU-containing cells was slower than the permeation in OmpT-containing cells. In addition, the OmpU-mediated outer membrane permeability was not affected by external bile, while the OmpT-mediated antibiotic flux was reduced by bile in a concentration-dependent manner. Our results confirm that OmpT and OmpU provide a passageway for hydrophilic solutes through the outer membrane and demonstrate that bile might interfere with this traffic in OmpT-producing cells by functionally inhibiting the OmpT pore. The insensitivity of OmpU to bile may be due to its small pore size and may provide an explanation for the resistance of OmpU-producing cells to bile in vivo.
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页码:121 / 126
页数:6
相关论文
共 27 条
[1]  
Benz Roland, 1997, Microbiologia (Madrid), V13, P321
[2]   Porins of Vibrio cholerae: Purification and characterization of OmpU [J].
Chakrabarti, SR ;
Chaudhuri, K ;
Sen, K ;
Das, J .
JOURNAL OF BACTERIOLOGY, 1996, 178 (02) :524-530
[3]   Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae [J].
Crawford, JA ;
Kaper, JB ;
DiRita, VJ .
MOLECULAR MICROBIOLOGY, 1998, 29 (01) :235-246
[4]   Polyamines decrease Escherichia coli outer membrane permeability [J].
delaVega, AL ;
Delcour, AH .
JOURNAL OF BACTERIOLOGY, 1996, 178 (13) :3715-3721
[5]  
DELCOUR AH, IN PRESS J MOL MICRO
[6]   REGULATORY CASCADE CONTROLS VIRULENCE IN VIBRIO-CHOLERAE [J].
DIRITA, VJ ;
PARSOT, C ;
JANDER, G ;
MEKALANOS, JJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (12) :5403-5407
[7]   Epidemiology, genetics, and ecology of toxigenic Vibrio cholerae [J].
Faruque, SM ;
Albert, MJ ;
Mekalanos, JJ .
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 1998, 62 (04) :1301-+
[8]   Bile affects production of virulence factors and motility of Vibrio cholerae [J].
Gupta, S ;
Chowdhury, R .
INFECTION AND IMMUNITY, 1997, 65 (03) :1131-1134
[9]   TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae [J].
Häse, CC ;
Mekalanos, JJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (02) :730-734
[10]   Complex inhibition of OmpF and OmpC bacterial porins by polyamines [J].
Iyer, R ;
Delcour, AH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (30) :18595-18601