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pubmed-article:20153694pubmed:abstractTextWe previously identified Legionella pneumophila PlaB as the major cell-associated phospholipase A/lysophospholipase A with contact-dependent hemolytic activity. In this study, we further characterized this protein and found it to be involved in the virulence of L. pneumophila. PlaB was mainly expressed and active during exponential growth. Active PlaB was outer membrane-associated and at least in parts surface-exposed. Transport to the outer membrane was not dependent on the type I (T1SS), II (T2SS), IVB (T4BSS) or Tat secretion pathways. Furthermore, PlaB activity was not dependent on the presence of the macrophage infectivity potentiator (Mip) or the major secreted zinc metalloproteinase A (MspA). Despite the fact that PlaB is not essential for replication in protozoa or macrophage cell lines, we found that plaB mutants were impaired for replication in the lungs and dissemination to the spleen in the guinea pig infection model. Histological sections monitored less inflammation and destruction of the lung tissue after infection with the plaB mutants compared to L. pneumophila wild type. Taken together, PlaB is the first phospholipase A/lysophospholipase A with a confirmed role in the establishment of Legionnaires' disease.lld:pubmed
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pubmed-article:20153694pubmed:copyrightInfoCopyright 2010 Elsevier GmbH. All rights reserved.lld:pubmed
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pubmed-article:20153694pubmed:articleTitlePhospholipase PlaB is a new virulence factor of Legionella pneumophila.lld:pubmed
pubmed-article:20153694pubmed:affiliationRobert Koch-Institut, Research Group P26, Nosocomial Infections of the Elderly, Nordufer 20, 13353 Berlin, Germany.lld:pubmed
pubmed-article:20153694pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20153694pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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