期刊
MOLECULAR MICROBIOLOGY
卷 43, 期 4, 页码 869-881出版社
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1365-2958.2002.02798.x
关键词
-
资金
- NIAID NIH HHS [AI33987] Funding Source: Medline
- NIGMS NIH HHS [T32GM07104] Funding Source: Medline
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 InIA 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 DeltasrtA mutant strain is defective in entering epithelial cells, similar to a DeltainIA mutant. In contrast to a DeltainIA mutant, the DeltasrtA 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 InIA and, presumably, for the anchoring of other LPXTG-containing proteins that are involved in listerial infections.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据