Vα domain modulates the multiple topologies of mouse T cell receptor Vβ20/staphylococcal enterotoxins A and E complexes

Autor: Y Bravo de Alba, Pierre-André Cazenave, Rafick Pierre Sekaly, Isabelle Cloutier, J Thibodeau, Patrice N. Marche
Rok vydání: 1997
Předmět:
Zdroj: European Journal of Immunology. 27:92-99
ISSN: 1521-4141
0014-2980
DOI: 10.1002/eji.1830270114
Popis: The superantigens staphylococcal enterotoxin A and E (SEA and SEE) both contact major histocompatibility complex (MHC) class II molecules on two sites located on the alpha and beta chains. We have investigated the role of the T cell receptor (TCR) alpha chain in the modulation of the various topologies of TCR/SEA (or SEE)/class II complexes. For this purpose, we have used three mouse V beta20 T cell lines expressing different V alpha domains and two T cell hybridomas expressing mouse V beta1 or V beta11 segments. The response of these T cells to SEA and SEE was studied in the context of presentation by wild-type human MHC class II molecules; or by mutants on MHC, in each of the two superantigen binding sites (position alpha39K and beta81H) to which the superantigens can still bind but with an altered conformation. Although V beta20 T cell lines are efficiently stimulated using SEA and SEE presented by wild-type HLA-DR1 molecules, our results show that the nature of the TCR V alpha domain can affect differently the recognition of the toxins bound to mutant class II molecules. This suggests that various functional topologies exist for both SEA and SEE/class II complexes and that the T cell response to each of these complexes can be modulated by the V alpha domain of the TCR. Interestingly, the recognition of SEA and SEE is achieved in different fashions by a given V beta20 T cell line.
Databáze: OpenAIRE