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“Background Sortases are membrane-bound cysteine transpeptidases that anchor surface proteins to the peptidoglycan cell wall in Gram-positive bacteria. Surface proteins buy RO4929097 anchored via sortases are often essential virulence factors important

in colonization and invasion, evasion of the host immune system, and nutrient acquisition. The sorting process is mediated by a conserved C-terminal cell wall sorting signal on the anchored protein, comprised of a C-terminal recognition sequence (often LPXTG, where X is any amino acid), followed closely by a hydrophobic transmembrane domain and a positively charged tail [1]. A conserved catalytic cysteine SGC-CBP30 in vivo residue of the sortase cleaves the LPXTG motif of the polypeptide between the threonine and glycine residues and covalently attaches the protein to the peptidoglycan MRIP [2–6]. There are six described sortase families, A-F, that share amino

acid similarity [7]. All catalyze similar transpeptidation reactions, but recognize different substrate motifs and serve different functions within the cell. Class A sortases (SrtA), such as the prototypical Staphylococcus aureus Sortase A (SaSrtA), are considered housekeeping sortases as they are capable of anchoring many functionally distinct proteins to the cell wall. SaSrtA, which recognizes an LPXTG motif, is responsible for anchoring a variety of surface proteins involved in adherence and immune response evasion, and is essential for virulence in animal models [8,9]. SrtA orthologues have been found in the genomes of almost all Gram-positive bacteria [8,10–16]. Class B sortases are functionally different from class A in their substrate specificity. In S. aureus and B.