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Proteins unique to intraphagosomally grown Mycobacterium tuberculosis
Author(s) -
Mattow Jens,
Siejak Frank,
Hagens Kristine,
Becher Dörte,
Albrecht Dirk,
Krah Alexander,
Schmidt Frank,
Jungblut Peter R.,
Kaufmann Stefan H. E.,
Schaible Ulrich E.
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500547
Subject(s) - phagosome , legionella pneumophila , biology , mycobacterium tuberculosis , microbiology and biotechnology , virulence , mycobacterium , tuberculosis , intracellular parasite , hypothetical protein , secretory protein , tandem mass tag , intracellular , phagocytosis , proteomics , bacteria , secretion , quantitative proteomics , biochemistry , gene , genetics , medicine , pathology
Pathogenic mycobacteria persist and replicate within phagosomes of host phagocytes by inhibiting phagosome maturation at an early endosome stage. The molecular basis for this behavior is not understood. To identify proteins of Mycobacterium tuberculosis unique to the intraphagosomal phase, mycobacteria were purified from phagosomes of infected murine bone marrow‐derived macrophages and analyzed by high‐resolution 2‐DE and MS. Protein patterns of intraphagosomally grown M. tuberculosis were compared with those of broth‐cultured mycobacteria. The analysis revealed 11 mycobacterial proteins exclusively detected in intraphagosomal mycobacteria. Some of these proteins are involved in metabolism and cell envelope synthesis, such as the lipid carrier protein Rv1627c, and the conserved hypothetical protein Rv1130 that shows homology to a virulence‐associated protein of Legionella pneumophila . The relevance of these proteins as factors enabling intracellular survival of M. tuberculosis is being discussed.