Selection of phage-displayed superantigen by binding to cell-surface MHC class II.
J Immunol Methods
; 204(1): 33-41, 1997 May 12.
Article
em En
| MEDLINE
| ID: mdl-9202707
ABSTRACT
We have expressed the superantigen staphylococcal enterotoxin A (SEA) on the surface of bacteriophage as a fusion with the gene VIII protein (gVIIIp). This phage-displayed superantigen retains the properties inherent in the natural protein. It binds to MHC class II and activates T-cells bearing appropriate V beta regions. A flexible 5-amino acid linker sequence between the SEA molecule and the phage coat protein improved the production of functional phage-displayed SEA. Binding to MHC class II-expressing cells effectively selected SEA-phage from non-SEA-phage background. This indicates that this will be an effective method for selecting new specificities of superantigen from libraries of SEA mutants and for cloning of novel superantigens.
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Base de dados:
MEDLINE
Assunto principal:
Bacteriófagos
/
Antígenos de Histocompatibilidade Classe II
/
Superantígenos
/
Enterotoxinas
/
Vetores Genéticos
Limite:
Animals
Idioma:
En
Ano de publicação:
1997
Tipo de documento:
Article