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What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)

Reactive antigenic epitopes on presumed autoantigens of biologic interest have been examined by many researchers. The central third complementarity-determining region (CDR3) residues of a human monoclonal anti-proteinase 3 (PR3) antibody contained many negatively charged aspartic acid residues, perh...

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Detalles Bibliográficos
Autores principales: Peen, Elisabeth, Ralph C, Williams
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2000
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC130014/
https://www.ncbi.nlm.nih.gov/pubmed/11094437
http://dx.doi.org/10.1186/ar97
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author Peen, Elisabeth
Ralph C, Williams
author_facet Peen, Elisabeth
Ralph C, Williams
author_sort Peen, Elisabeth
collection PubMed
description Reactive antigenic epitopes on presumed autoantigens of biologic interest have been examined by many researchers. The central third complementarity-determining region (CDR3) residues of a human monoclonal anti-proteinase 3 (PR3) antibody contained many negatively charged aspartic acid residues, perhaps contributing to its reactivity with positively charged PR3 regions. Examination of four other human monoclonal anti-PR3 antibodies shows a number of negatively charged residues within their CDR3 regions. Mapping of segments of linear PR3-epitopes reacting with anti-neutrophil cytoplasmic antibodies (ANCA) demonstrated a preliminary estimate of structures contributing to antigenic determinants. T-cell epitopes on PR3 are reported in studies of chronic myeloid leukemia. These T-cell epitopes appear to be human leukocyte antigen (HLA) A2.1 restricted.
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spelling pubmed-1300142002-10-28 What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3) Peen, Elisabeth Ralph C, Williams Arthritis Res Review Reactive antigenic epitopes on presumed autoantigens of biologic interest have been examined by many researchers. The central third complementarity-determining region (CDR3) residues of a human monoclonal anti-proteinase 3 (PR3) antibody contained many negatively charged aspartic acid residues, perhaps contributing to its reactivity with positively charged PR3 regions. Examination of four other human monoclonal anti-PR3 antibodies shows a number of negatively charged residues within their CDR3 regions. Mapping of segments of linear PR3-epitopes reacting with anti-neutrophil cytoplasmic antibodies (ANCA) demonstrated a preliminary estimate of structures contributing to antigenic determinants. T-cell epitopes on PR3 are reported in studies of chronic myeloid leukemia. These T-cell epitopes appear to be human leukocyte antigen (HLA) A2.1 restricted. BioMed Central 2000 2000-06-12 /pmc/articles/PMC130014/ /pubmed/11094437 http://dx.doi.org/10.1186/ar97 Text en Copyright © 2000 Current Science Ltd
spellingShingle Review
Peen, Elisabeth
Ralph C, Williams
What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)
title What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)
title_full What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)
title_fullStr What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)
title_full_unstemmed What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)
title_short What you should know about PR3-ANCA: Structural aspects of antibodies to proteinase 3 (PR3)
title_sort what you should know about pr3-anca: structural aspects of antibodies to proteinase 3 (pr3)
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC130014/
https://www.ncbi.nlm.nih.gov/pubmed/11094437
http://dx.doi.org/10.1186/ar97
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