| pubmed-article:14982622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14982622 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:14982622 | lifeskim:mentions | umls-concept:C0023861 | lld:lifeskim |
| pubmed-article:14982622 | lifeskim:mentions | umls-concept:C0042765 | lld:lifeskim |
| pubmed-article:14982622 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:14982622 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:14982622 | lifeskim:mentions | umls-concept:C0142292 | lld:lifeskim |
| pubmed-article:14982622 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:14982622 | pubmed:dateCreated | 2004-2-25 | lld:pubmed |
| pubmed-article:14982622 | pubmed:abstractText | Most bacteria contain one type I signal peptidase (Spase I) for cleavage of signal peptides from exported and secreted proteins. Here, we identified a locus encoding three contiguous Spase I genes in the genome of Listeria monocytogenes. The deduced Sip proteins (denoted SipX, SipY and SipZ) are significantly similar to SipS and SipT, the major SPase I proteins of Bacillus subtilis (38% to 44% peptidic identity). We studied the role of these multiple signal peptidases in bacterial pathogenicity by constructing a series of single- and double-chromosomal knock-out mutants. Inactivation of sipX did not affect intracellular multiplication of L. monocytogenes but significantly reduced bacterial virulence (approximately 100-fold). Inactivation of sipZ impaired the secretion of phospholipase C (PC-PLC) and listeriolysin O (LLO), restricted intracellular multiplication and almost abolished virulence (LD(50) of 10(8.3)), inactivation of sipY had no detectable effects. Most importantly, a mutant expressing only SipX was impaired in intracellular survival and strongly attenuated in the mouse (LD(50) of 10(7.2)), whereas, a mutant expressing only SipZ behaved like wild-type EGD in all the assays performed. The data establish that SipX and SipZ perform distinct functions in bacterial pathogenicity and that SipZ is the major Spase I of L. monocytogenes. This work constitutes the first report on the differential role of multiple Spases I in a pathogenic bacterium and suggests a possible post-translational control mechanism of virulence factors expression. | lld:pubmed |
| pubmed-article:14982622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14982622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14982622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14982622 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14982622 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:BerchePatrick... | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:Réglier-Poupe... | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:DubailIharila... | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:CharbitAlainA | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:FrehelClaudeC | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:RaynaudCather... | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:LetyMarie-Ann... | lld:pubmed |
| pubmed-article:14982622 | pubmed:author | pubmed-author:BonnemainClai... | lld:pubmed |
| pubmed-article:14982622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14982622 | pubmed:volume | 51 | lld:pubmed |
| pubmed-article:14982622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14982622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14982622 | pubmed:pagination | 1251-66 | lld:pubmed |
| pubmed-article:14982622 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:14982622 | pubmed:meshHeading | pubmed-meshheading:14982622... | lld:pubmed |
| pubmed-article:14982622 | pubmed:meshHeading | pubmed-meshheading:14982622... | lld:pubmed |
| pubmed-article:14982622 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14982622 | pubmed:articleTitle | Differential roles of multiple signal peptidases in the virulence of Listeria monocytogenes. | lld:pubmed |
| pubmed-article:14982622 | pubmed:affiliation | INSERM U-570, CHU Necker-Enfants Malades, 156, rue de Vaugirard, 75730 Paris Cedex 15-France. | lld:pubmed |
| pubmed-article:14982622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14982622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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