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Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence
Author(s) -
Bierne Hélène,
Mazmanian Sarkis K.,
Trost Matthias,
Pucciarelli M. Graciela,
Liu Gwen,
Dehoux Pierre,
Jänsch Lothar,
Portillo Francisco Garciadel,
Schneewind Olaf,
Cossart Pascale
Publication year - 2002
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2002.02798.x
Subject(s) - listeria monocytogenes , biology , peptidoglycan , mutant , sortase , sortase a , virulence , gene , microbiology and biotechnology , signal peptide , protein sorting signals , phenotype , cell wall , bacteria , peptide sequence , genetics , bacterial protein
Summary During infection of their hosts, Gram‐positive bac‐teria 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 Δ srtA mutant strain is defective in entering epithelial cells, similar to a Δ inlA mutant. In contrast to a Δ inlA mutant, the Δ 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.