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Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence
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 ge...
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Published in: | Molecular microbiology 2002-02, Vol.43 (4), p.869-881 |
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Main Authors: | , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 ΔsrtA mutant strain is defective
in entering epithelial cells, similar to a ΔinlA mutant. In contrast
to a ΔinlA mutant, the ΔsrtA 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. |
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ISSN: | 0950-382X 1365-2958 |
DOI: | 10.1046/j.1365-2958.2002.02798.x |