A mouse monoclonal antibody against rabbit V<sub>H</sub> allotype shares the predominant idiotype with a rabbit antibody of the same specificity

Metzger, Dennis W.

doi:10.1002/eji.1830140405

Cited by 8 publications

(3 citation statements)

References 22 publications

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“…The UBl peptide, bearing no homology to the above peptides, was used as a control. The peptides were tested for the ability to inhibit the binding of rabbit al Ig to an anti-al mAb, 3-2F1, which recognizes the common al allotope (9). The assay was performed by preincubating the inhibitors in Ab-coated wells for 24 h before addition of 1251al Ig .…”

Section: Resultsmentioning

confidence: 99%

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Do antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?

Cleave

Naeve

Metzger

1988

The Journal of Experimental Medicine

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An integral component within Jerne's idiotype network theory (1) is the internal image antibody (Ab) 1 that bears determinants within the variable (V) region resembling external antigens . Internal images mimicking viruses, bacteria, protozoa, and natural ligands have been described (2-5) and have generated interest in their use as potential vaccines and probes for cellular receptors (6). The structural basis for internal image expression, however, remains largely unknown. Two recent studies using the synthetic (Glub°Ala 3°Tyrt°) terpolymer (7) and the reovirus hemagglutinin (8) have identified determinants in Ab internal image V regions that appear to match linear or continuous sequences within each respective antigen. Further insight into the molecular nature of internal images and the rules that govern antigen recognition will be crucial for the rational design of internal image vaccines and an understanding of idiotypic interactions .To investigate internal image expression in a well-defined protein system, we have used the al allotype of rabbit Ig as a model antigen (9-11) and have isolated two mouse mAbs that bear al-like determinants within their antigen-binding sites (12). We have now obtained the V region amino acid sequences of these internal images and have found that both mAbs contain a unique sequence of identity with rabbit Ig but in a novel configuration. The data, coupled with results from synthetic peptide inhibition experiments, indicate that an amino acid sequence oriented in reverse direction on an internal image molecule can effectively mimic the nominal antigen .

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Section: Resultsmentioning

confidence: 99%

“…Radioimmunoassay. Polyvinyl microtiter wells (Dynatech Laboratories, Inc., Alexandria, VA) were coated with 100 ul of 100 wg/ml affinity-purified 3-2F1, a mouse IgGl mAb specific for the common al allotope (9). Unbound protein was recovered and the plates were washed three times with 0.01 M PBS, pH 7.0, containing 1% (wt/vol) BSA (Sigma Chemical Co ., St .…”

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confidence: 99%

Do antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?

Cleave

Naeve

Metzger

1988

The Journal of Experimental Medicine

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“…Rabbit anti-allotype Ab and anti-Id Ab were prepared as previously reported [6,11,121. The production and characterization of the mouse monoclonal Ab (3-2F1) to an a1 allotope has also been described [13].…”

Section: Ab Productionmentioning

confidence: 99%

Induced latent allotypes within rabbit anti‐crossreactive idiotype reagents. Direct immunoelectron microscopic evidence

et al. 1984

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Immunization of rabbits with anti-VHa allotype antibody leads to the production of an "anti-cross-reactive idiotype (IdX)" reagent which appears to recognize a highly conserved IdX on anti-allotype antibodies. In many rabbits, a large percentage of this "anti-IdX" reagent does not express the nominal VHa framework allotype of the rabbit from which it was derived and is otherwise serologically indistinguishable from the original antigen, i.e. a1 or a2 allotype. To determine whether these anti-IdX molecules were in fact anti-IdX (or internal images) or were induced immunoglobulins bearing latent VHa allotypes, immunoelectron microscopic analysis of the molecules in complex with Fab anti-allotype antibody was conducted. The results show that the complexes do not resemble idiotype-anti-idiotype interactions but are essentially indistinguishable from allotype-anti-allotype complexes. We conclude that a major component of the "anti-idiotype" response of these anti-VHa-immunized rabbits is the production of Ig molecules bearing latent VHa allotypes.

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Mouse monoclonal antibodies induced by anti‐allotype antibody display internal images of the rabbit V_Ha1 allotype: Direct visualization by immunoelectron microscopy

1986

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We have previously shown that injection of adult rabbits with anti-immunoglobulin (Ig) antibody (Ab) induces the expression of genetically unexpected Ig markers, i.e., a1 allotypic determinants. We now show that these rabbit Ig markers can also be induced in mice by a similar treatment; in the latter case the a1 determinants are located in the antigen-combining site and thus represent "internal images". Two monoclonal antibodies (mAb) were developed from mice treated with anti-allotype Ab. These mAb were reactive with all homologous and heterologous anti-a1 Ab but not normal Ig; efficiently inhibited the binding of rabbit a1 Ig to anti-a1 Ab; and elicited the production of anti-allotype Ab when injected into normal mice. To determine whether the a1-like determinants on these mAb were located in the antigen-combining site, immunoelectron microscopy was utilized to directly visualize Ab complexes. Complexes composed of intact Ab and anti-a1 Fab fragments yielded uniform binding patterns which were identical to those produced by anti-idiotypic reactions. In each case, an identical tip-to-tip binding configuration was observed with a single Fab fragment attached at an approximate 180 degree angle to the V region terminus of each Ab arm. In contrast, rabbit a1 Ig bound as many as two anti-a1 fragments per Ig arm; these fragments were attached laterally and at right angles to the intact molecule. These mAb thus provide the first direct evidence that Ab2 beta determinants are located in, or near, the antigen-combining site.

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A mouse monoclonal antibody against rabbit V_H allotype shares the predominant idiotype with a rabbit antibody of the same specificity

Cited by 8 publications

References 22 publications

Do antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?

Do antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?

Induced latent allotypes within rabbit anti‐crossreactive idiotype reagents. Direct immunoelectron microscopic evidence

Mouse monoclonal antibodies induced by anti‐allotype antibody display internal images of the rabbit V_Ha1 allotype: Direct visualization by immunoelectron microscopy

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A mouse monoclonal antibody against rabbit VH allotype shares the predominant idiotype with a rabbit antibody of the same specificity

Cited by 8 publications

References 22 publications

Do antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?

Do antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?

Induced latent allotypes within rabbit anti‐crossreactive idiotype reagents. Direct immunoelectron microscopic evidence

Mouse monoclonal antibodies induced by anti‐allotype antibody display internal images of the rabbit VHa1 allotype: Direct visualization by immunoelectron microscopy

Contact Info

Product

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A mouse monoclonal antibody against rabbit V_H allotype shares the predominant idiotype with a rabbit antibody of the same specificity

Mouse monoclonal antibodies induced by anti‐allotype antibody display internal images of the rabbit V_Ha1 allotype: Direct visualization by immunoelectron microscopy