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Galactan-binding antibodies. Diversity and structure of idiotypes

A group of eight IgM hybridoma proteins induced with beta(1,6)-D- galactan-containing antigens has been characterized in terms of primary amino acid sequence and idiotype expression. The H chain amino acid sequences reveal very strong homology in the VH segment although several substitutions are see...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187133/
https://www.ncbi.nlm.nih.gov/pubmed/6195282
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description A group of eight IgM hybridoma proteins induced with beta(1,6)-D- galactan-containing antigens has been characterized in terms of primary amino acid sequence and idiotype expression. The H chain amino acid sequences reveal very strong homology in the VH segment although several substitutions are seen that suggest the occurrence of somatic mutation in these IgM molecules. Significant sequence variation was observed in CDR-3, the region generated by the D segment, and the two recombination events, VH-D and D-JH. The number of amino acids in this region contributed by the D segment was found to vary from two to six, yet the overall length of CDR-3 was precisely maintained by the addition of amino acids on either side of D during the recombination processes. These additional amino acids are suggested to result from nucleotide addition by repair enzymes. Idiotypic analysis of these proteins, in conjunction with an assessment of the H chain sequences, has permitted an identification of the molecular basis of both cross- reacting and unique idiotypic determinants expressed by these molecules.
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spelling pubmed-21871332008-04-17 Galactan-binding antibodies. Diversity and structure of idiotypes J Exp Med Articles A group of eight IgM hybridoma proteins induced with beta(1,6)-D- galactan-containing antigens has been characterized in terms of primary amino acid sequence and idiotype expression. The H chain amino acid sequences reveal very strong homology in the VH segment although several substitutions are seen that suggest the occurrence of somatic mutation in these IgM molecules. Significant sequence variation was observed in CDR-3, the region generated by the D segment, and the two recombination events, VH-D and D-JH. The number of amino acids in this region contributed by the D segment was found to vary from two to six, yet the overall length of CDR-3 was precisely maintained by the addition of amino acids on either side of D during the recombination processes. These additional amino acids are suggested to result from nucleotide addition by repair enzymes. Idiotypic analysis of these proteins, in conjunction with an assessment of the H chain sequences, has permitted an identification of the molecular basis of both cross- reacting and unique idiotypic determinants expressed by these molecules. The Rockefeller University Press 1983-11-01 /pmc/articles/PMC2187133/ /pubmed/6195282 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Galactan-binding antibodies. Diversity and structure of idiotypes
title Galactan-binding antibodies. Diversity and structure of idiotypes
title_full Galactan-binding antibodies. Diversity and structure of idiotypes
title_fullStr Galactan-binding antibodies. Diversity and structure of idiotypes
title_full_unstemmed Galactan-binding antibodies. Diversity and structure of idiotypes
title_short Galactan-binding antibodies. Diversity and structure of idiotypes
title_sort galactan-binding antibodies. diversity and structure of idiotypes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187133/
https://www.ncbi.nlm.nih.gov/pubmed/6195282