Alloreactive T cells recognize a complex composed of an allogenek major histocompatibility complex (MHC) molecule and a peptide derived from the processing of nonpolymorphic proteins. A sizable fraction of MHC class II alloreactive T cells is shown to recognize peptides derived from constitutive processing of human serum protons. One such ephope is a fragment of human serum albumin. This epitope bound selectively to the human class II molecule DRw11 and was constitutively present on antigen-presenting cells in vivo. These data indicate that, in the case of MHC class II, peptides involved in allorecognition may originate from exogenous proteins.

Recognition by class II alloreactive T cells of processed determinants from human serum proteins / Panina-Bordignon, P.; Corradin, G.; Roosnek, E.; Sette, A.; Lanzavecchia, A.. - In: SCIENCE. - ISSN 0036-8075. - 252:5012(1991), pp. 1548-1550. [10.1126/science.1710827]

Recognition by class II alloreactive T cells of processed determinants from human serum proteins

Panina-Bordignon P.;
1991-01-01

Abstract

Alloreactive T cells recognize a complex composed of an allogenek major histocompatibility complex (MHC) molecule and a peptide derived from the processing of nonpolymorphic proteins. A sizable fraction of MHC class II alloreactive T cells is shown to recognize peptides derived from constitutive processing of human serum protons. One such ephope is a fragment of human serum albumin. This epitope bound selectively to the human class II molecule DRw11 and was constitutively present on antigen-presenting cells in vivo. These data indicate that, in the case of MHC class II, peptides involved in allorecognition may originate from exogenous proteins.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.11768/105564
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