NDLI: The antibody response to an HLA mismatch: a model for nonself-self discrimination in relation to HLA epitope immunogenicity.

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The antibody response to an HLA mismatch: a model for nonself-self discrimination in relation to HLA epitope immunogenicity.

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The antibody response to an HLA mismatch: a model for nonself-self discrimination in relation to HLA epitope immunogenicity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Duquesnoy, R. J.
Description	Country affiliation: United States Author Affiliation: Duquesnoy RJ ( Department of PathologyThe Thomas E Starzl Transplantation Institute, University of Pittsburgh Medical Center, Pittsburgh, PA 15213, USA. Duquesnoyr@upmc.edu)
Abstract	Antibodies to HLA mismatches are specific for epitopes rather than antigens. HLAMatchmaker considers each HLA antigen as a string of eplets that represent key elements of epitopes. Certain antibodies are specific for single eplets, but recent studies have demonstrated that epitopes defined by eplet pairs always involve one nonself-eplet and a self-eplet shared between the immunizing antigen and the antibody producer. This suggests an autoreactive component of the alloantibody response to an HLA mismatch and this report expands this concept. During B-cell development, V(H) and V(L) gene rearrangements produce a diversity of Ig receptors that can recognize epitopes on autologous proteins. It is hypothesized that B cells carry low-affinity receptors for self-HLA antigens. Their interactions with self-HLA proteins will not lead to B-cell activation or antibody production. In contrast, exposure to HLA mismatches induces often strong alloantibody responses. The activation of self-HLA-specific B cell by a nonself-eplet may require that the remainder of the structural epitope of the immunizing antigen has considerable structural similarity with one of the antibody producer's alleles. This hypothesis has been tested in molecular modelling studies with six epitopes defined by human monoclonal antibodies. In each case, one allele of the antibody producer had no or few differences with the immunizing allele in antibody-accessible positions defined by a 15 Ångstrom radius of the mismatched eplet. The other alleles of the antibody producer showed significantly greater numbers of residue differences with the immunizer (5.8 ± 2.0 versus 1.0 ± 0.6, P < 0.0001). These data support the concept that HLA antibodies originate from B cells with self-HLA immunoglobulin receptors that recognize mismatched eplets as nonself entities on immunizing antigens. The nonself-self paradigm provides a new insight of HLA epitope immunogenicity and may explain why sensitized patients have antibodies to a restricted number of mismatched epitopes.
File Format	HTM / HTML
ISSN	17443121
Issue Number	1
Volume Number	39
e-ISSN	1744313X
Journal	International Journal of Immunogenetics
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2012-02-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Genetics Discipline Immunology Antibody Formation Epitopes Immunology Hla Antigens Models, Immunological Alleles Antibodies, Monoclonal Genetics Antibody Specificity B-lymphocytes Blood Transfusion Gene Rearrangement, B-lymphocyte Humans Isoantibodies Journal Article Review
Content Type	Text
Resource Type	Article
Subject	Genetics Molecular Biology Immunology Genetics (clinical)

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