Source:http://linkedlifedata.com/resource/pubmed/id/14982622
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2004-2-25
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors,
http://linkedlifedata.com/resource/pubmed/chemical/type I signal peptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1251-66
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:14982622-Amino Acid Sequence,
pubmed-meshheading:14982622-Animals,
pubmed-meshheading:14982622-Bacterial Proteins,
pubmed-meshheading:14982622-Genome, Bacterial,
pubmed-meshheading:14982622-Humans,
pubmed-meshheading:14982622-Isoenzymes,
pubmed-meshheading:14982622-Listeria monocytogenes,
pubmed-meshheading:14982622-Listeriosis,
pubmed-meshheading:14982622-Macrophages,
pubmed-meshheading:14982622-Membrane Proteins,
pubmed-meshheading:14982622-Mice,
pubmed-meshheading:14982622-Molecular Sequence Data,
pubmed-meshheading:14982622-Mutation,
pubmed-meshheading:14982622-Sequence Alignment,
pubmed-meshheading:14982622-Serine Endopeptidases,
pubmed-meshheading:14982622-Type C Phospholipases,
pubmed-meshheading:14982622-Virulence Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Differential roles of multiple signal peptidases in the virulence of Listeria monocytogenes.
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pubmed:affiliation |
INSERM U-570, CHU Necker-Enfants Malades, 156, rue de Vaugirard, 75730 Paris Cedex 15-France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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