Understanding antibiotic permeation through OccD3 of Pseudomonas aeruginosa

  • Pseudomonas aeruginosa utilizes a plethora of substrate specific channels for the uptake of small nutrients. OccD3 (OpdP or PA4501) is an OprD-like arginine uptake channel of P. aeruginosa whose role has been implicated in carbapenem uptake. To understand the mechanism of selective permeation, we reconstituted single OccD3 channels in a planar lipid bilayer and characterized the interaction with Imipenem and Meropenem, analyzing the ion current fluctuation in the presence of substrates. We performed point mutations in the constriction region of OccD3 to understand the binding and translocation of antibiotic in OccD3. By mutating two key residues in the substrate binding sites of OccD3 (located in the internal loop L7 and basic ladder), we emphasize the importance of these residues. We show that carbapenem antibiotics follow a similar path as arginine through the constriction zone and the basic ladder to translocate across OccD3.

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Publishing Institution:IRC-Library, Information Resource Center der Jacobs University Bremen
Granting Institution:Jacobs Univ.
Author:Gowrishankar Soundararajan
Referee:Mathias Winterhalter, Richard Wagner, Björn Windshügel
Advisor:Mathias Winterhalter
Persistent Identifier (URN):urn:nbn:de:gbv:579-opus-1007226
Document Type:PhD Thesis
Language:English
Date of Successful Oral Defense:2017/06/28
Date of First Publication:2017/07/07
Academic Department:Life Sciences & Chemistry
PhD Degree:Biochemical Engineering
Focus Area:Health
Call No:Thesis 2017/11

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