alexa Proteome Dynamics of the Specialist Oxalate Degrader Ox
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Proteome Dynamics of the Specialist Oxalate Degrader Oxalobacter formigenes

Mellissa L Ellis, James A Mobley, Ross P Holmes, John Knight*

Department of Urology, University of Alabama at Birmingham, Birmingham, AL, USA

*Corresponding Author:
John Knight
Department of Urology
University of Alabama at Birmingham
Kaul 816B, 1720 20th street south
Birmingham, AL 35294, USA
Tel: 205-996-2295
E-mail: [email protected]

Received Date: November 16, 2015 Accepted Date: January 26, 2016 Published Date: January 29, 2016

Citation: Ellis ML, Mobley JA, Holmes RP, Knight J (2016) Proteome Dynamics of the Specialist Oxalate Degrader Oxalobacter formigenes. J Proteomics Bioinform 9:019-025. doi:10.4172/jpb.1000384

Copyright: © 2016 Ellis ML, 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.



Oxalobacter formigenes is a unique intestinal organism that relies on oxalate degradation to meet most of its energy and carbon needs. A lack of colonization is a risk factor for calcium oxalate kidney stone disease. The release of the genome sequence of O. formigenes has provided an opportunity to increase our understanding of the biology of O. formigenes. This study used mass spectrometry based shotgun proteomics to examine changes in protein levels associated with the transition of growth from log to stationary phase. Of the 1867 unique protein coding genes in the genome of O. formigenes strain OxCC13, 1822 proteins were detected, which is at the lower end of the range of 1500-7500 proteins found in free-living bacteria. From the protein datasets presented here it is clear that O. formigenes contains a repertoire of metabolic pathways expected of an intestinal microbe that permit it to survive and adapt to new environments. Although further experimental testing is needed to confirm the physiological and regulatory processes that mediate adaptation with nutrient shifts, the O. formigenes protein datasets presented here can be used as a reference for studying proteome dynamics under different conditions and have significant potential for hypothesis development.


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