Bacillus anthracis Sortase A (SrtA) anchors LPXTG motif-containing surface proteins to the cell wall envelope

被引:65
作者
Gaspar, AH
Marraffini, LA
Glass, EM
DeBord, KL
Ton-That, H
Schneewind, O
机构
[1] Univ Chicago, Dept Microbiol, Chicago, IL 60637 USA
[2] Univ Chicago, Dept Mol Genet & Cell Biol, Chicago, IL 60637 USA
[3] Argonne Natl Lab, Div Math & Comp Sci, Argonne, IL 60439 USA
关键词
D O I
10.1128/JB.187.13.4646-4655.2005
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Cell wall-anchored surface proteins of gram-positive pathogens play important roles during the establishment of many infectious diseases, but the contributions of surface proteins to the pathogenesis of anthrax have not yet been revealed. Cell wall anchoring in Staphylococcus aureus occurs by a transpeptidation mechanism requiring surface proteins with C-terminal sorting signals as well as sortase enzymes. The genome sequence of Bacillus anthracis encodes three sortase genes and eleven surface proteins with different types of cell wall sorting signals. Purified B. anthracis sortase A cleaved peptides encompassing LPXTG motif-type sorting signals between the threonine (T) and the glycine (G) residues in vitro. Sortase A activity could be inhibited by thiol-reactive reagents, similar to staphylococcal sortases. B. anthracis parent strain Sterne 34F(2), but not variants lacking the srt4 gene, anchored the collagen-binding MSCRAMM (microbial surface components recognizing adhesive matrix molecules) BasC (BA5258/BAS4884) to the bacterial cell wall. These results suggest that B. anthracis SrtA anchors surface proteins bearing LPXTG motif sorting signals to the cell wall envelope of vegetative bacilli.
引用
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页码:4646 / 4655
页数:10
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