Continued proteomic analysis of Mycobacterium leprae subcellular fractions

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...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2004-10, Vol.4 (10), p.2942-2953
Main Authors: 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.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Bacterial Proteins - chemistry
Basic proteins
Biological and medical sciences
Chromatography, Affinity
Cytosol - metabolism
Dasypus
Electrophoresis, Gel, Two-Dimensional
Fundamental and applied biological sciences. Psychology
Genome, Bacterial
Mass Spectrometry
Miscellaneous
Mycobacterium leprae
Mycobacterium leprae - metabolism
Proteins
Proteome
Proteomics - methods
Spectrometry, Mass, Electrospray Ionization
Subcellular fractions
Subcellular Fractions - metabolism
Two-dimensional gel electrophoresis
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Summary: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 pI > 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.
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.200400945