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Microbiology 147 (2001), 3135-3140
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Microbiology (2001), 147, 3135-3140.
© 2001 Society for General Microbiology

Pathogenicity and Medical Microbiology

Substrate-specific diffusion of select dicarboxylates through Chlamydia trachomatis PorB

Aya Kubo1 and Richard S. Stephens1,2

Division of Infectious Diseases, School of Public Health, 140 Earl Warren Hall, University of California, Berkeley, CA 94720, USA1
Francis I. Proctor Foundation, University of California, San Francisco, CA 94143, USA2

Author for correspondence: Richard S. Stephens. Tel: +1 510 643 9900. Fax: +1 510 643 1537. e-mail: rss{at}uclink4.berkeley.edu

Chlamydiae contain two porins, MOMP and PorB, that facilitate diffusion of solutes through the outer membrane. MOMP is a general porin that permits the diffusion of a wide variety of compounds including carbohydrates and amino acids. The relative inefficiency of PorB as a general porin and its low abundance in the outer membrane suggest that it may function as a substrate-specific porin. The tricarboxylic acid (TCA) cycle of chlamydiae is incomplete and to function would require the exogenous acquisition of 2-oxoglutarate or glutamate. A liposome-swelling assay for anions as well as an enzyme-linked liposome assay were used to demonstrate the efficient diffusion of dicarboxylates such as 2-oxoglutarate through PorB. These data demonstrate that PorB is a dicarboxylate-specific porin that may feed the chlamydial TCA cycle and provide chlamydiae with carbon and energy production intermediates.

Keywords: major outer-membrane protein, porin, 2-oxoglutarate

Abbreviations: MOMP, major outer-membrane protein; TCA cycle, tricarboxylic acid cycle




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