Cargando…

HLA-E: A Novel Player for Histocompatibility

The classical class I human leukocyte antigens (HLA-A, -B, and -C) present allele-specific self- or pathogenic peptides originated by intracellular processing to CD8(+) immune effector cells. Even a single mismatch in the heavy chain (hc) of an HLA class I molecule can impact on the peptide binding...

Descripción completa

Detalles Bibliográficos
Autores principales: Kraemer, Thomas, Blasczyk, Rainer, Bade-Doeding, Christina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4221882/
https://www.ncbi.nlm.nih.gov/pubmed/25401109
http://dx.doi.org/10.1155/2014/352160
_version_ 1782342943791644672
author Kraemer, Thomas
Blasczyk, Rainer
Bade-Doeding, Christina
author_facet Kraemer, Thomas
Blasczyk, Rainer
Bade-Doeding, Christina
author_sort Kraemer, Thomas
collection PubMed
description The classical class I human leukocyte antigens (HLA-A, -B, and -C) present allele-specific self- or pathogenic peptides originated by intracellular processing to CD8(+) immune effector cells. Even a single mismatch in the heavy chain (hc) of an HLA class I molecule can impact on the peptide binding profile. Since HLA class I molecules are highly polymorphic and most of their polymorphisms affect the peptide binding region (PBR), it becomes obvious that systematic HLA matching is crucial in determining the outcome of transplantation. The opposite holds true for the nonclassical HLA class I molecule HLA-E. HLA-E polymorphism is restricted to two functional versions and is thought to present a limited set of highly conserved peptides derived from class I leader sequences. However, HLA-E appears to be a ligand for the innate and adaptive immune system, where the immunological response to peptide-HLA-E complexes is dictated through the sequence of the bound peptide. Structural investigations clearly demonstrate how subtle amino acid differences impact the strength and response of the cognate CD94/NKG2 or T cell receptor.
format Online
Article
Text
id pubmed-4221882
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-42218822014-11-16 HLA-E: A Novel Player for Histocompatibility Kraemer, Thomas Blasczyk, Rainer Bade-Doeding, Christina J Immunol Res Review Article The classical class I human leukocyte antigens (HLA-A, -B, and -C) present allele-specific self- or pathogenic peptides originated by intracellular processing to CD8(+) immune effector cells. Even a single mismatch in the heavy chain (hc) of an HLA class I molecule can impact on the peptide binding profile. Since HLA class I molecules are highly polymorphic and most of their polymorphisms affect the peptide binding region (PBR), it becomes obvious that systematic HLA matching is crucial in determining the outcome of transplantation. The opposite holds true for the nonclassical HLA class I molecule HLA-E. HLA-E polymorphism is restricted to two functional versions and is thought to present a limited set of highly conserved peptides derived from class I leader sequences. However, HLA-E appears to be a ligand for the innate and adaptive immune system, where the immunological response to peptide-HLA-E complexes is dictated through the sequence of the bound peptide. Structural investigations clearly demonstrate how subtle amino acid differences impact the strength and response of the cognate CD94/NKG2 or T cell receptor. Hindawi Publishing Corporation 2014 2014-10-20 /pmc/articles/PMC4221882/ /pubmed/25401109 http://dx.doi.org/10.1155/2014/352160 Text en Copyright © 2014 Thomas Kraemer et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Kraemer, Thomas
Blasczyk, Rainer
Bade-Doeding, Christina
HLA-E: A Novel Player for Histocompatibility
title HLA-E: A Novel Player for Histocompatibility
title_full HLA-E: A Novel Player for Histocompatibility
title_fullStr HLA-E: A Novel Player for Histocompatibility
title_full_unstemmed HLA-E: A Novel Player for Histocompatibility
title_short HLA-E: A Novel Player for Histocompatibility
title_sort hla-e: a novel player for histocompatibility
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4221882/
https://www.ncbi.nlm.nih.gov/pubmed/25401109
http://dx.doi.org/10.1155/2014/352160
work_keys_str_mv AT kraemerthomas hlaeanovelplayerforhistocompatibility
AT blasczykrainer hlaeanovelplayerforhistocompatibility
AT badedoedingchristina hlaeanovelplayerforhistocompatibility