Abstract:
:Sortases are transamidases that covalently link proteins to the peptidoglycan of gram-positive bacteria. The genome of the pathogenic bacterium Listeria monocytogenes encodes two sortases genes, srtA and srtB. The srtA gene product anchors internalin and some other LPXTG-containing proteins to the listerial surface. Here, we focus on the role of the second sortase, SrtB. Whereas SrtA acts on most of the proteins in the peptidoglycan fraction, SrtB appears to target minor amounts of surface polypeptides. We identified one of the SrtB-anchored proteins as the virulence factor SvpA, a surface-exposed protein which does not contain the LPXTG motif. Therefore, as in Staphylococcus aureus, the listerial SrtB represents a second class of sortase in L. monocytogenes, involved in the attachment of a subset of proteins to the cell wall, most likely by recognizing an NXZTN sorting motif. The DeltasrtB mutant strain does not have defects in bacterial entry, growth, or motility in tissue-cultured cells and does not show attenuated virulence in mice. SrtB-mediated anchoring could therefore be required to anchor surface proteins involved in the adaptation of this microorganism to different environmental conditions.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Bierne H,Garandeau C,Pucciarelli MG,Sabet C,Newton S,Garcia-del Portillo F,Cossart P,Charbit Adoi
10.1128/jb.186.7.1972-1982.2004keywords:
subject
Has Abstractpub_date
2004-04-01 00:00:00pages
1972-82issue
7eissn
0021-9193issn
1098-5530journal_volume
186pub_type
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doi:10.1128/jb.177.1.206-211.1995
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更新日期:1998-04-01 00:00:00
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更新日期:2006-12-01 00:00:00
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更新日期:1985-04-01 00:00:00