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- W2155171508 endingPage "141" @default.
- W2155171508 startingPage "128" @default.
- W2155171508 abstract "The rise in antibiotic-resistant bacteria is a major concern, in particular because it includes many different species of pathogenic microbes. These superbugs are further characterized by high levels of virulence and disease-associated mortality. There seems to be few new antibiotics in the drug discovery pipeline; recent work has sought to define and validate new drug targets. The assembly of surface proteins and pili in the cell wall envelope of Gram-positive bacteria is catalyzed by sortase. Sortase cleaves a conserved C-terminal sequence of these polypeptides to generate an acyl-enzyme intermediate. The acyl-enzyme is next resolved by nucleophilic attack by the amino groups within cell wall cross-bridges or pilin proteins, thereby covalently attaching the polypeptides to the cell wall or the next pilin subunit. Sortase substrates function as adhesins, internalins, blood clotting and immune evasion factors, and transporters for nutrients across the microbial cell wall envelope; without them, most pathogens cannot sustain an infection. Here we review what is known about sortase catalysis and surface protein function, how surface protein anchoring can be inhibited, and what prospects such inhibition may have for anti-infective therapy." @default.
- W2155171508 created "2016-06-24" @default.
- W2155171508 creator A5006264387 @default.
- W2155171508 creator A5083683183 @default.
- W2155171508 date "2008-03-01" @default.
- W2155171508 modified "2023-10-14" @default.
- W2155171508 title "Sortase as a Target of Anti-Infective Therapy" @default.
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