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Molecular & Cellular Proteomics 2:1284-1296, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Comprehensive Proteomic Profiling of the Membrane Constituents of a Mycobacterium tuberculosis Strain^*,S

Sheng Gu, Jin Chen, Karen M. Dobos, E. Morton Bradbury^,¶, John T. Belisle and Xian Chen^,||

From the Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87544, the Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado 80523, and the ^¶ Department of Biological Chemistry, School of Medicine, University of California, Davis, California 95616

Mycobacterium tuberculosis is an infectious microorganism that causes human tuberculosis. The cell membranes of pathogens are known to be rich in possible diagnostic and therapeutic protein targets. To compliment the M. tuberculosis genome, we have profiled the membrane protein fraction of the M. tuberculosis H37Rv strain using an analytical platform that couples one-dimensional SDS gels to a microcapillary liquid chromatography-nanospray-tandem mass spectrometer. As a result, 739 proteins have been identified by two or more distinct peptide sequences and have been characterized. Interestingly, 450 proteins represent novel identifications, 79 of which are membrane proteins and more than 100 of which are membrane-associated proteins. The physicochemical properties of the identified proteins were studied in detail, and then biological functions were obtained by sorting them according to Sanger Institute gene function category. Many membrane proteins were found to be involved in the cell envelope, and those proteins with energy metabolic functions were also identified in this study.

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