| Literature DB >> 14595687 |
Jens Mattow1, Ulrich E Schaible, Frank Schmidt, Kristine Hagens, Frank Siejak, Gordon Brestrich, Gisela Haeselbarth, Eva-Christina Müller, Peter R Jungblut, Stefan H E Kaufmann.
Abstract
A comprehensive analysis of culture supernatant (CSN) proteins of Mycobacterium tuberculosis H37Rv was accomplished by combination of two-dimensional electrophoresis (2-DE), mass spectrometry, and N-terminal sequencing by Edman degradation. Analytical 2-DE gels resolved approximately 1250 protein spots from CSN of M. tuberculosis H37Rv, 381 of which were identified by mass spectrometry and/or Edman degradation. This study revealed 137 different proteins, 42 of which had previously been described as secreted. Comparative proteome analysis of CSN from virulent M. tuberculosis H37Rv and attenuated Mycobacterium bovis BCG Copenhagen identified 39 M. tuberculosis-specific spots containing 27 different proteins, representing candidate antigens for novel vaccines and diagnostics in tuberculosis. These included five proteins encoded by open reading frames absent from M. bovis BCG, e.g., early secretory antigen target (Esat6), as well as 22 novel differential proteins, such as acetyl-CoA C-acetyltransferase (Rv0243) and two putative Esat6-like proteins (Rv1198, Rv1793).Entities:
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Year: 2003 PMID： 14595687 DOI： 10.1002/elps.200305601
Source DB: PubMed Journal: Electrophoresis ISSN： 0173-0835 Impact factor: 3.535