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Identification of an intracellular M17 family leucine aminopeptidase that is required for virulence in Staphylococcus aureus

Författare och institution:
R. K. Carroll (-); T. M. Robison (-); F. E. Rivera (-); J. E. Davenport (-); Ing-Marie Jonsson (Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning); D. Florczyk (-); Andrej Tarkowski (Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning); J. Potempa (-); J. Koziel (-); L. N. Shaw (-)
Publicerad i:
Microbes and Infection, 14 ( 11 ) s. 989-999
Artikel, refereegranskad vetenskaplig
Sammanfattning (abstract):
Staphylococcus aureus is a highly virulent bacterial pathogen capable of causing a variety of ailments throughout the human body. It is a major public health concern due to the continued emergence of highly pathogenic methicillin resistant strains (MRSA) both within hospitals and in the community. Virulence in S. aureus is mediated by an array of secreted and cell wall associated virulence factors, including toxins, hemolysins and proteases. In this work we identify a (l) under bar eucine (a) under bar mino (p) under bar eptidase (LAP, pepZ) that strongly impacts the pathogenic abilities of S. aureus. Disruption of the pepZ gene in either Newman or USA300 resulted in a dramatic attenuation of virulence in both localized and systemic models of infection. LAP is required for survival inside human macrophages and gene expression analysis shows that pepZ expression is highest in the intracellular environment. We examine the cellular location of LAP and demonstrate that it is localized to the bacterial cytosol. These results identify for the first time an intracellular leucine aminopeptidase that influences disease causation in a Gram-positive bacterium. (C) 2012 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
Medicinska grundvetenskaper ->
Immunologi inom det medicinska området
Leucine aminopeptidase, LAP, Virulence, Peptidase, Staphylococcus, site-specific recombination, lactic-acid bacteria, escherichia-coli, systemic infection, bacillus-subtilis, peptidase-n, gene, pepa, inactivation, macrophages, arlier d, 1995, journal of molecular biology, v250, p392
Postens nummer:
Posten skapad:
2012-10-30 17:09

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