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- Title
Superantigenic activity of toxic shock syndrome toxin-1 is resistant to heating and digestive enzymes.
- Authors
Li, S.-J.; Hu, D.-L.; Maina, E.K.; Shinagawa, K.; Omoe, K.; Nakane, A.
- Abstract
To elucidate the stability of superantigenic activity and pathogenesis of toxic shock syndrome toxin 1 (TSST-1) and staphylococcal enterotoxin A (SEA) against heating and digestive enzymes. Purified TSST-1 and SEA were treated with heating, pepsin and trypsin that are related to food cooking, stomach and intestine conditions. The integrity, superantigenic activity and toxicity of treated TSST-1 and SEA were analysed by Western blotting, spleen cell culture, cytokine assay and toxic shock models. Both TSST-1 and SEA showed strong resistance to heating, pepsin and trypsin digestion. Furthermore, the treated TSST-1 showed significant higher induction of interferon-γ and toxic shock compared with that of SEA. Pepsin- or trypsin-digested TSST-1 fragments still showed significant superantigenic and lethal shock toxicities. The superantigenic activity of TSST-1 was stable to heating and digestive enzymes. Pepsin- and trypsin-digested TSST-1 fragments still showed superantigenic and lethal shock activities, indicating that digested TSST-1 could cross epithelial cells and induce systemic toxicity. This study found, for the first time, that pepsin- or trypsin-digested smaller TSST-1 retained significant superantigenic and lethal shock activities. The different resistance of TSST-1 and SEA participates in the different pathogenic activities during food poisoning and toxic shock syndrome.
- Subjects
TOXIC shock syndrome; DIGESTIVE enzymes; STAPHYLOCOCCAL diseases; CELL culture; EPITHELIAL cells; FOOD poisoning; THERAPEUTICS
- Publication
Journal of Applied Microbiology, 2011, Vol 110, Issue 3, p729
- ISSN
1364-5072
- Publication type
Article
- DOI
10.1111/j.1365-2672.2010.04927.x