Recurrent idiotopes and internal images.

Jerne, Niels K.; Roland, Jacques; Cazenave, Pierre-André

doi:10.1002/j.1460-2075.1982.tb01154.x

Cited by 412 publications

(167 citation statements)

References 48 publications

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“…28 and 29) and the apparent production of idiotype-positive antibodies by animals that are lacking the presumed variable region gene required for idiotype expression (30). One explanation for these phenomena may be that polyclonal anti-idiotypic antibodies against conformation-dependent determinants on immunoglobulins often contain a minor component with the "internal image" of the antigen (31)(32)(33)(34) Additionally, monoclonal anti-idiotope reagents may crossreact with substances that share a conformational determinant with idiotype-positive immunoglobulins in spite of a distinct primary structure (36,37). By comparison, the HVPinduced anti-idiotypic antibody is free of internal image components and may crossreact with substances that include a region of similar primary structure.…”

Section: Discussionmentioning

confidence: 99%

Anti-hypervariable region antibody induced by a defined peptide: an approach for studying the structural correlates of idiotypes.

Chen¹,

Houghten²,

Fong³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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The structural correlates of idiotypes have been sought in several antibody systems. However, the precise molecular basis of idiotypes are exceedingly difficult to define.Antibodies of predetermined specificity can be induced by immunization with synthetic peptides. In the present experiments, a synthetic peptide corresponding to a hypervariable region on a monoclonal human IgM rheumatoid factor (Sie) has been used to induce specific anti-hypervariable region antibodies. The antibodies bound to the intact Ig molecule and to its isolated heavy chains but not to other IgM paraproteins nor to pooled human IgG. The binding of the antibody to the intact IgM was inhibited specifically by the free peptide, and the antibody activity was removed by a peptide-coupled affrmity column. These results clearly demonstrate that specific antiidiotypic antibody of predefined specificity can be induced by a hypervariable region peptide. Antibodies of this class may provide a new tool for defining the structural correlates of idiotypes.The study of idiotypes (1) has greatly advanced our understanding of immunoglobulin genetics and antibody structure (2, 3). In addition, idiotypes have been postulated to play an essential role in the generation and regulation of diverse immune responses (4-6).The structural correlates of idiotypes have been sought in several well-defined antibody systems (7)(8)(9)(10)(11)(12). Because of the common occurrence of monoclonal human IgM paraproteins with anti-IgG activity (rheumatoid factors), the idiotypes and the primary amino acid sequences of these proteins were compared in detail (9, 10, 13). The heavy and light chains from two monoclonal IgM rheumatoid factors (IgM-RF) with crossreactive idiotypes (e.g., Lay and Pom) had identical amino acid sequences in three of six complementarity-determining regions but differed substantially in the framework regions (9, 10). These results suggested that the hypervariable regions of the heavy and light chains were the structural correlates of idiotypic determinants. Similar comparisons of amino acid sequences and idiotypes among mouse monoclonal antibodies with antigen binding activity have yielded much the same conclusions (8,11,12). Noticeably, in the murine anti-Dextran system, one private idiotype and one public idiotype were assigned, respectively, to the third and the second hypervariable region of the heavy chain (11). However, in most other cases, it has proven to be extremely difficult to associate a particular idiotypic determinant with a specific amino acid sequence (7 MATERIALS AND METHODSPreparation of Synthetic Peptide. Peptides were prepared by the solid-phase method (17-20), using a Beckman model 990B peptide synthesizer. Briefly, 1.00 g (ca. 0.5 milliequivalent) of N-t-butoxycarbonylglutamic acid (BocGlu) resin was used along with the following side-chain protecting groups: O-bromobenzyloxycarbonyl for tyrosine and lysine; O-benzyl for glutamic acid and aspartic acid; S-methoxybenzyl for cysteine. Protected amino acids were recrystalli...

show abstract

Section: Discussionmentioning

confidence: 99%

Anti-hypervariable region antibody induced by a defined peptide: an approach for studying the structural correlates of idiotypes.

Chen¹,

Houghten²,

Fong³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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show abstract

“…Jerne et al (1982) have classified anti-idiotype antibodies according to the location of the idiotype recognization in their early report, and two main types of antiidiotype antibodies have been distinguished: alphatype ( -AId) and betatype ( -AId). By definition, -AId recognizes an epitope within the framework of the variable region of the primary antibody, but is not sensitive to the presence or absence of the analyte at the binding site.…”

Section: Anti-idiotype Antibody Based Noncompetitive Immunoassay (Idimentioning

confidence: 99%

Recent Progress in Noncompetitive Hapten Immunoassays: A Review

Fan¹

2012

Trends in Immunolabelled and Related Techniques

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“…Id-anti-Id interactions may, or may not, be inhibitable by antigen (2). In addition to these types of anti-Id antibodies, which will be referred to as classical anti-Ids, there are also internal image anti-Ids (13) and epibodies (14).…”

Section: Composition Of the B-cell Establishmentmentioning

confidence: 99%

“…For example, as pointed out by Jerne et al (13), it is possible that some internal image antibodies can image two or more determinants. The more S-determinants imaged by an establishment clone the higher its rank is likely to be.…”

Section: Composition Of the B-cell Establishmentmentioning

confidence: 99%

Crime and Punishment in the Society of Lymphocytes: A Speculation on the Structure of the Putative Idiotypic Network

Cleveland¹

1988

Anti-Idiotypes, Receptors, and Molecular Mimicry

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Recurrent idiotopes and internal images.

Cited by 412 publications

References 48 publications

Anti-hypervariable region antibody induced by a defined peptide: an approach for studying the structural correlates of idiotypes.

Anti-hypervariable region antibody induced by a defined peptide: an approach for studying the structural correlates of idiotypes.

Recent Progress in Noncompetitive Hapten Immunoassays: A Review

Crime and Punishment in the Society of Lymphocytes: A Speculation on the Structure of the Putative Idiotypic Network

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