†Present address: Committee on Microbiology, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA.
Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence
Article first published online: 27 MAR 2002
Volume 43, Issue 4, pages 869–881, February 2002
How to Cite
Bierne, H., Mazmanian, S. K., Trost, M., Pucciarelli, M. G., Liu, G., Dehoux, P., the European Listeria Genome Consortium, Jänsch, L., Portillo, F. G.-d., Schneewind, O. and Cossart, P. (2002), Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence. Molecular Microbiology, 43: 869–881. doi: 10.1046/j.1365-2958.2002.02798.x
- Issue published online: 27 MAR 2002
- Article first published online: 27 MAR 2002
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.