UCL logo

UCL Discovery

UCL home » Library Services » Electronic resources » UCL Discovery

The structural basis of T-cell allorecognition

Whitelegg, A; Barber, LD; (2004) The structural basis of T-cell allorecognition. TISSUE ANTIGENS , 63 (2) pp. 101-108.

Full text not available from this repository.

Abstract

Foreign allogeneic major histocompatibility complex (MHC) class I and class II molecules elicit an exceptionally vigorous T-cell response. A small component of the alloresponse comprises CD4+ T cells that recognize allogeneic MHC indirectly after processing into peptide fragments that are bound and presented by self-MHC class II. The majority of alloreactive T cells directly recognize intact allogeneic MHC molecules expressed on foreign cells. Some alloreactive T-cell interactions with allogeneic MHC molecules are indifferent to the bound peptide, but evidence suggests that most show specificity to peptide. The vigor and diversity of the direct alloreactive T-cell response can therefore be explained by summation of numerous responses to each of the peptides in the novel set bound by allogeneic MHC molecules. Structural studies definitively show that the overall mechanism of T-cell receptor (TCR) recognition of self-MHC and allogeneic MHC molecules is similar. Many alloreactive T cells recognize several different combinations of MHC and bound peptide that do not necessarily possess structural homology. Flexibility within the TCR structure allows adaptation to the different contact surfaces. Crossreactivity seems to be an intrinsic property of the TCR required, because a single TCR must possess the ability to interact with both self-MHC during positive selection and at least one combination of foreign antigenic peptide presented by self-MHC. Recognition of allogeneic MHC molecules is an inadvertent consequence of the need for TCR crossreactivity

Type: Article
Title: The structural basis of T-cell allorecognition
Additional information: Language: EnglishSubset: IMJournal code: 0000331072Document status: MedlinePublication model: PrintDataStar source field: Tissue antigens, {Tissue-Antigens}, Feb 2004, vol. 63, no. 2, p. 101-8, 70 refs, ISSN: 0001-2815DataStar update date: 20050101
Keywords: 0 (Isoantigens), 0 (Receptors-Antigen-T-Cell), ANIMALS, antigen, ANTIGENS, CELLS, CLASS-I, histocompatibility-complex, hospital, HUMANS, ISOANTIGENS/*CH (chemistry), IM (immunology), language, LONDON, major-histocompatibility-complex, MAJOR-HISTOCOMPATIBILITY-COMPLEX/*IM (immunology), MEDLINE, model, MOLECULES, peptide, PROTEIN-CONFORMATION, publication, receptor, RECEPTORS-ANTIGEN-T-CELL/*IM (immunology), RESEARCH-SUPPORT-NON-U-S-GOVT, SURFACE, T-LYMPHOCYTES/*IM (immunology)
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute > Research Department of Haematology
URI: http://discovery.ucl.ac.uk/id/eprint/181939
Downloads since deposit
0Downloads
Download activity - last month
Download activity - last 12 months
Downloads by country - last 12 months

Archive Staff Only

View Item View Item