PubMed ID

22272184

UMMS Affiliation

Program in Molecular Medicine

Date

1-17-2012

Document Type

Article

Subjects

Bacterial Outer Membrane Proteins; Ion Channels; Multigene Family; Porins; Pseudomonas aeruginosa

Disciplines

Biochemistry, Biophysics, and Structural Biology | Life Sciences | Medicine and Health Sciences

Abstract

Many Gram-negative bacteria, including human pathogens such as Pseudomonas aeruginosa, do not have large-channel porins. This results in an outer membrane (OM) that is highly impermeable to small polar molecules, making the bacteria intrinsically resistant towards many antibiotics. In such microorganisms, the majority of small molecules are taken up by members of the OprD outer membrane protein family. Here we show that OprD channels require a carboxyl group in the substrate for efficient transport, and based on this we have renamed the family Occ, for outer membrane carboxylate channels. We further show that Occ channels can be divided into two subfamilies, based on their very different substrate specificities. Our results rationalize how certain bacteria can efficiently take up a variety of substrates under nutrient-poor conditions without compromising membrane permeability. In addition, they explain how channel inactivation in response to antibiotics can cause resistance but does not lead to decreased fitness.

Comments

Citation: Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, et al. (2012) Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10(1): e1001242. doi:10.1371/journal.pbio.1001242. Link to article on publisher's site

Copyright: © 2012 Eren et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Related Resources

Link to Article in PubMed