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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.