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Bacillus anthracis Sortase A (SrtA) Anchors LPXTG Motif-Containing Surface Proteins to the Cell Wall Envelope

Andrew H. Gaspar,^1, Luciano A. Marraffini,² Elizabeth M. Glass,³ Kristin L. DeBord,¹ Hung Ton-That,^1, and Olaf Schneewind^1*

Department of Microbiology,¹ Department of Molecular Genetics & Cell Biology, University of Chicago, 920 East 58th Street, Chicago, Illinois,² Mathematics and Computer Sciences Division, Argonne National Laboratory, Argonne, Illinois³

Received 22 January 2005/ Accepted 25 March 2005

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 34F₂, but not variants lacking the srtA 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.

Present address: Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030.

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