Superantigenic activity of toxic shock syndrome toxin-1 is resistant to heating and digestive enzymes.
J Appl Microbiol
; 110(3): 729-36, 2011 Mar.
Article
em En
| MEDLINE
| ID: mdl-21255209
ABSTRACT
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 ANDRESULTS:
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.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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Toxinas Bacterianas
/
Tripsina
/
Pepsina A
/
Superantígenos
/
Enterotoxinas
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Temperatura Alta
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article