Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence

Hélène Bierne, Sarkis K. Mazmanian, Matthias Trost, M. Graciela Pucciarelli, Gwen Liu, Pierre Dehoux, Lothar Jänsch, Francisco Garcia-del Portillo, Olaf Schneewind, Pascale Cossart, European Listeria Genome Consortium

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    178 Citations (Scopus)


    During infection of their hosts, Gram-positive bacteria express surface proteins that serve multiple biological functions. Surface proteins harbouring a C-terminal sorting signal with an LPXTG motif are covalently linked to the cell wall peptidoglycan by a transamidase named sortase. Two genes encoding putative sortases, termed srtA and srtB, were identified in the genome of the intracellular pathogenic bacterium Listeria monocytogenes. Inactivation of srtA abolishes anchoring of the invasion protein InlA to the bacterial surface. It also prevents the proper sorting of several other peptidoglycan-associated LPXTG proteins. Three were identified by a mass spectrometry approach. The ?srtA mutant strain is defective in entering epithelial cells, similar to a ?inlA mutant. In contrast to a ?inlA mutant, the ?srtA mutant is impaired for colonization of the liver and spleen after oral inoculation in mice. Thus, L. monocytogenes srtA is required for the cell wall anchoring of InlA and, presumably, for the anchoring of other LPXTG-containing proteins that are involved in listerial infections.

    Original languageEnglish
    Pages (from-to)869-81
    Number of pages13
    JournalMolecular Microbiology
    Issue number4
    Publication statusPublished - 2002


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