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Molecular localization of human IgG anti-F(ab′)2 reactivity with variable- and constant-region λ light-chain epitopes

Identifieur interne : 000127 ( Istex/Curation ); précédent : 000126; suivant : 000128

Molecular localization of human IgG anti-F(ab′)2 reactivity with variable- and constant-region λ light-chain epitopes

Auteurs : Ralph C. Williams Jr. [États-Unis] ; Christine C. Malone [États-Unis] ; Franco Silvestris [États-Unis] ; Alan Solomon [États-Unis]

Source :

Journal of Clinical Immunology [ 0271-9142 ] ; 1995-11-01.

RBID : ISTEX:0D77452CF4BC31C4F0AEB5E42CBC0B38CEDCF2E1

English descriptors

Abstract

Abstract: Human IgG antibodies reacting with antigenic determinants on F(ab′)2 fragments represent generic antiidiotypic antibodies present in the serum of normal individuals. Additionally, the titers of these antibodies in the sera of patients with systemic lupus erythematosus (SLE) are inversely related to disease activity. Because these autoantibodies recognize predominantly light chain-related epitopes, especially λ type, we synthesized constant (C)λ- and variable (V)λ-related overlapping 7-mer peptides on polypropylene pins to determine anti-F(ab′)2-reactive epitopes on humanλ light chains. ELISA reactivity of affinity-purified anti-F(ab′)2 antibodies obtained from normal individuals and from patients with SLE, as well as murine anti-human light-chain monoclonal antibodies specific for Cλ and Vλ subgroup-related determinants, was tested using the overlapping 7-mers of humanλ light-chain sequence. The patterns of reactivity against Cλ-related peptides were similar in both normal and SLE-derived anti-F(ab′)2 antibodies. However, reactivity profiles against Vλ-related peptides were distinctively different between the normal and the SLE-associated anti-F(ab′)2 autoantibodies. A decrease in reactivity among the SLE IgG anti-F(ab′)2 antibodies was noted for particular amino acid Vλ complementarity-determining region (CDR) residues, including glycine at positions 27 and 54, alanine at 16 and 37, and tyrosine at 28 and 91. This different pattern of reactivity from normal may indicate that in SLE there is a failure of antiidiotypic control mechanisms, as reflected by a defect in production of antibody to immunodominant Vλ CDR residues.

Url:

https://api.istex.fr/ark:/67375/1BB-6S3PFTD3-4/fulltext.pdf

DOI: 10.1007/BF01541325

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Idiotypes (Ids)</term>
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<term>autoantibodies</term>
<term>systemic lupus erythematosus</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Affinity chromatography</term>
<term>Affinity measurements</term>
<term>Alanine</term>
<term>Alanine substitution strategy</term>
<term>Amino</term>
<term>Amino acid</term>
<term>Amino acid residues</term>
<term>Amino acids</term>
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<term>Antibody preparations</term>
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<term>Antigenic determinants</term>
<term>Antigenic epitopes</term>
<term>Arth rheum</term>
<term>Average affinity</term>
<term>Average elisa reactivity</term>
<term>Bence jones protein</term>
<term>Boldface type</term>
<term>Clin</term>
<term>Clin immunol immunopathol</term>
<term>Clinical immunology</term>
<term>Competition elisa</term>
<term>Conformational epitopes</term>
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<term>Elisa</term>
<term>Elisa reactivity</term>
<term>Elisa reactivity profile</term>
<term>Epitope</term>
<term>Framework regions</term>
<term>Glycine</term>
<term>Higher values</term>
<term>Human antibodies</term>
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<term>Immunodominant residues</term>
<term>Immunol</term>
<term>Immunol methods</term>
<term>Immunology</term>
<term>Inhibition enzyme immunoassay</term>
<term>Inhibition studies</term>
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<term>Light chain epitopes</term>
<term>Light chains</term>
<term>Linear epitopes</term>
<term>Linear regions</term>
<term>Mabs</term>
<term>Major importance</term>
<term>Malone</term>
<term>Maximum binding concentration</term>
<term>Maximum inhibition</term>
<term>Molecular localization</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Normal donor</term>
<term>Normal individuals</term>
<term>Normal subject</term>
<term>Normal subjects</term>
<term>Peptide</term>
<term>Polypropylene pins</term>
<term>Positive reactions</term>
<term>Reactive</term>
<term>Reactive epitopes</term>
<term>Reactive peaks</term>
<term>Reactive peptides</term>
<term>Reactive profile</term>
<term>Reactive regions</term>
<term>Reactivity profile</term>
<term>Reactivity profiles</term>
<term>Reagent</term>
<term>Residue</term>
<term>Rheumatoid</term>
<term>Rheumatoid arthritis</term>
<term>Rheumatoid factors</term>
<term>Room temperature</term>
<term>Serial dilutions</term>
<term>Silvestris</term>
<term>Strong reactivity</term>
<term>Substitution</term>
<term>Substitution technique</term>
<term>Synthetic peptides</term>
<term>Systemic lupus erythematosus</term>
<term>Variable region</term>
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<front><div type="abstract" xml:lang="en">Abstract: Human IgG antibodies reacting with antigenic determinants on F(ab′)2 fragments represent generic antiidiotypic antibodies present in the serum of normal individuals. Additionally, the titers of these antibodies in the sera of patients with systemic lupus erythematosus (SLE) are inversely related to disease activity. Because these autoantibodies recognize predominantly light chain-related epitopes, especially λ type, we synthesized constant (C)λ- and variable (V)λ-related overlapping 7-mer peptides on polypropylene pins to determine anti-F(ab′)2-reactive epitopes on humanλ light chains. ELISA reactivity of affinity-purified anti-F(ab′)2 antibodies obtained from normal individuals and from patients with SLE, as well as murine anti-human light-chain monoclonal antibodies specific for Cλ and Vλ subgroup-related determinants, was tested using the overlapping 7-mers of humanλ light-chain sequence. The patterns of reactivity against Cλ-related peptides were similar in both normal and SLE-derived anti-F(ab′)2 antibodies. However, reactivity profiles against Vλ-related peptides were distinctively different between the normal and the SLE-associated anti-F(ab′)2 autoantibodies. A decrease in reactivity among the SLE IgG anti-F(ab′)2 antibodies was noted for particular amino acid Vλ complementarity-determining region (CDR) residues, including glycine at positions 27 and 54, alanine at 16 and 37, and tyrosine at 28 and 91. This different pattern of reactivity from normal may indicate that in SLE there is a failure of antiidiotypic control mechanisms, as reflected by a defect in production of antibody to immunodominant Vλ CDR residues.</div>
</front>
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Molecular localization of human IgG anti-F(ab′)2 reactivity with variable- and constant-region λ light-chain epitopes

Molecular localization of human IgG anti-F(ab′)2 reactivity with variable- and constant-region λ light-chain epitopes

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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