Superantigenic activity of toxic shock syndrome toxin-1 is resistant to heating and digestive enzymes

作者：Li, S. -J.; Hu, D. -L.; Maina, E. K.; Shinagawa, K.; Omoe, K.; Nakane, A.^*

来源：Journal of Applied Microbiology, 2011, 110(3): 729-736.

DOI：10.1111/j.1365-2672.2010.04927.x

• emesis
• resistance
• staphylococcal enterotoxin
• superantigen
• toxic shock syndrome toxin 1

Aims:
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.
Methods and Results:
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-gamma and toxic shock compared with that of SEA. Pepsin- or trypsin-digested TSST-1 fragments still showed significant superantigenic and lethal shock toxicities.
Conclusions:
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.
Significance and Impact of the Study:
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.

• 出版日期2011-3
• 单位中国医科大学