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PMID:15458407
| Citation |
Coye, LH and Collins, CM (2004) Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes. Mol. Microbiol. 54:89-98 |
|---|---|
| Abstract |
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. SpyA, MW 24.9, has amino acid identity with the ADP-riboslytransferases (ADPRTs) Staphylococcus aureus EDIN and Clostridium botulinum C3. Recombinant SpyA was able to hydrolyse beta-NAD(+), and this activity was dependent on a glutamate at position 187. SpyA has a putative biglutamate active site, and similar to most biglutamate ADPRTs, was able to ADP-ribosylate poly-l-arginine. SpyA modified numerous proteins in both CHO and HeLa cell lysates. Two-dimesional gel analysis and MALDI-TOF MS analysis of modified proteins indicated that vimentin, tropomyosin and actin, all cytoskeletal proteins, are targets. Expression of spyA in HeLa cells resulted in loss of actin microfilaments. We hypothesize that SpyA is produced by S. pyogenes to disrupt cytoskeletal structures and promote colonization of the host. |
| Links |
PubMed Online version:10.1111/j.1365-2958.2004.04262.x |
| Keywords |
ADP Ribose Transferases/chemistry; ADP Ribose Transferases/genetics; ADP Ribose Transferases/metabolism; Amino Acid Sequence; Animals; CHO Cells; Cricetinae; Cytoskeletal Proteins/metabolism; HeLa Cells; Humans; Molecular Sequence Data; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Streptococcus pyogenes/chemistry; Streptococcus pyogenes/enzymology; Streptococcus pyogenes/pathogenicity |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0016757: transferase activity, transferring glycosyl groups |
ECO:0000315: |
F |
Mutant phenotype was inferred based on Figure 4, in which SpyA was assayed for the ability to ADP-ribosylate arginine. As shown, there was labelled precipitated material when SpyA was incubated with poly-l-arginine and only limited precipitated radioactive material with the active site mutant SpyA-E187A. |
complete | ||||
|
enables |
GO:0016757: transferase activity, transferring glycosyl groups |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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