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Continued proteomic analysis of Mycobacterium leprae subcellular fractions
Author(s) -
Marques Maria Angela M.,
Espinosa Benjamin J.,
Xavier da Silveira Erika K.,
Pessolani Maria Cristina V.,
Chapeaurouge Alex,
Perales Jonas,
Dobos Karen M.,
Belisle John T.,
Spencer John S.,
Brennan Patrick J.
Publication year - 2004
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.200400945
Subject(s) - mycobacterium leprae , biology , proteomics , gene , bacteria , microbiology and biotechnology , genome , mycobacterium , biochemistry , context (archaeology) , genetics , paleontology , leprosy , immunology
Abstract Recently the sequence of the Mycobacterium leprae chromosome, the only known obligate intracellular mycobacterium, was completed. It has a dramatic reduction in functional genes, with a coding capacity of only 49.5%, the lowest one so far observed among bacterial genomes. The leprosy bacillus seems to preserve a minimal set of genes that allows its survival in the host. The identification of genes that are actually expressed by the bacterium is of high significance in the context of mycobacterial pathogenesis. In this current study, a proteomic approach was undertaken to identify the proteins present in the soluble/cytosol and membrane subcellular fractions obtained from armadillo derived M. leprae. Proteins from each fraction were separated by two‐dimensional gel electrophoresis (2‐DE) and identified by mass spectrometry. A total of 147 protein spots were identified from 2‐DE patterns and shown to comprise products of 44 different genes, twenty eight of them corresponding to new proteins. Additionally, two highly basic proteins (with p I > 10.0) were isolated by heparin affinity chromatography and identified by N ‐terminal sequencing. This study constitutes the first application of proteomics to a host‐derived Mycobacterium .