Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes.
作者： Lisette H. Coye , Carleen M. Collins
DOI: 10.1111/J.1365-2958.2004.04262.X
关键词:
摘要: Streptococcus pyogenes, the aetiological agent of both respiratory and skin infections, produces numerous exotoxins to establish infection. This report identifies a new exotoxin produced by this organism, termed SpyA, for S. pyogenesADP-ribosylating toxin. MW 24.9, has amino acid identity with ADP-riboslytransferases (ADPRTs) Staphylococcus aureus EDIN Clostridium botulinum C3. Recombinant SpyA was able hydrolyse beta-NAD(+), activity dependent on glutamate at position 187. putative biglutamate active site, similar most ADPRTs, ADP-ribosylate poly-l-arginine. modified proteins in CHO HeLa cell lysates. Two-dimesional gel analysis MALDI-TOF MS indicated that vimentin, tropomyosin actin, all cytoskeletal proteins, are targets. Expression spyA cells resulted loss actin microfilaments. We hypothesize is pyogenes disrupt structures promote colonization host.
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