Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/28951
Title: Deciphering the proteomic profile of Mycobacterium leprae cell envelope
Authors: Marques, Maria Angela M.
Ferreira, Ana Gisele C. Neves
Silveira, Erika K. Xavier da
Valente, Richard H.
Chapeaurouge, Alexander
Perales, Jonas
Bernardes, Renato da Silva
Dobos, Karen M.
Spencer, John S.
Brennan, Patrick J.
Pessolani, Maria Cristina V.
Affilliation: Colorado State University. Department of Microbiology, Immunology and Pathology. Fort Collins, CO, USA.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil.
Colorado State University. Department of Microbiology, Immunology and Pathology. Fort Collins, CO, USA.
Colorado State University. Department of Microbiology, Immunology and Pathology. Fort Collins, CO, USA.
Colorado State University. Department of Microbiology, Immunology and Pathology. Fort Collins, CO, USA.
Colorado State University. Department of Microbiology, Immunology and Pathology. Fort Collins, CO, USA.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Microbiologia Celular. Rio de Janeiro, RJ, Brasil.
Abstract: The complete sequence of the Mycobacterium leprae genome, an obligate intracellular pathogen, shows a dramatic reduction of functional genes, with a coding capacity of less than 50%. Despite this massive gene decay, the leprosy bacillus has managed to preserve a minimal gene set, most of it shared with Mycobacterium tuberculosis, allowing its survival in the host with ensuing pathological manifestations. Thus, the identification of proteins that are actually expressed in vivo by M. leprae is of high significance in understanding obligate, intracellular mycobacterial pathogenesis. In this study, a high-throughput proteomic approach was undertaken resulting in the identification of 218 new M. leprae proteins. Of these, 60 were in the soluble/cytosol fraction, 98 in the membrane and 104 in the cell wall. Although several proteins were identified in more than one subcellular fraction, the majority were unique to one. As expected, a high percentage of these included enzymes responsible for lipid biosynthesis and degradation, biosynthesis of the major components of the mycobacterial cell envelope, proteins involved in transportation across lipid barriers, and lipoproteins and transmembrane proteins with unknown functions. The data presented in this study contribute to our understanding of the in vivo composition and physiology of the mycobacterial cell envelope, a compartment known to play a major role in bacterial pathogenesis.
Keywords: Cell envelope
Mycobacterium leprae
Pathogenesis
Subcellular compartments
keywords: Mycobacterium leprae
Patogênese
Compartimentos subcelulares
Issue Date: 2008
Publisher: Wiley
Citation: MARQUES, Maria Angela M. et al. Deciphering the proteomic profile of Mycobacterium leprae cell envelope. Proteomics, v.8, p.2477-2491, 2008.
DOI: 10.1002/pmic.200700971
ISSN: 1615-9853
Copyright: restricted access
Appears in Collections:IOC - Artigos de Periódicos

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