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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...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2000
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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 |
Sumario: | 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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