Surface proteins of Gram-positive pathogens are key determinants of virulence that
substantially shape host-microbe interactions. Specifically, these proteins mediate host …

Staphylococcus aureus and Staphylococcus epidermidis are two of the most significant
opportunistic human pathogens, causing medical implant and nosocomial infections …

Sortase enzymes are attractive targets for the development of new anti-infective agents
against Gram-positive pathogens because they covalently anchor virulence factors to the …

Gram-positive bacterial pathogens have an array of proteins on their cell surface that
mediate interactions with the host environment. In particular, bacterial cell wall-associated …

Sortases cleave short peptide motif sequences at the C-terminal end of secreted surface
protein precursors and either attach these polypeptides to the peptidoglycan of Gram …

Gram-positive pathogenic bacteria dis-play proteins on their surface that may interact with
host cells and tissues and play a role in virulence. How these proteins are targeted through …

The surface of Staphylococcus aureus is decorated with over 20 proteins that are covalently
anchored to peptidoglycan by the action of sortase A. These cell wall-anchored (CWA) …

Sortase A (SrtA) is a cysteine transpeptidase of most Gram-positive bacteria that is
responsible for the anchorage of many surface protein virulence factors to the cell wall layer …

During the bacteriumYhost cell interaction, bacterial surface proteins play a key role in the
pathogenesis of disease. These proteins expressed in various sizes and shape on the …

Staphylococcus aureus sortase A cleaves surface protein precursors bearing C-terminal
LPXTG motif sorting signals between the threonine and glycine residues. Using lipid II …