Immunogenicity of Synthetic Polymers of Amino Acids; Role of Carrier and Genetic Background

Maurer, Paul H.; Pinchuck, Paul

doi:10.1016/b978-1-4832-2762-7.50024-8

Cited by 7 publications

(4 citation statements)

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“…The genetic segregation of the ability of anti-(Phe, G)-Pro--L sera from (DBA/1 X SJL) F1 X DBA/1 and (DBA/1 X S J-L) F1 X SJL mice to bind (T,G)-Pro--L and (Phe, G)-A--L will be reported in a subsequent publication. 1 Evidence leading to a similar conclusion has been reported by Arquilla and Finn (17) and Maurer and Pinchuck (18).…”

Section: Ref 5)supporting

confidence: 71%

The Nature of the Antigenic Determinant in a Genetic Control of the Antibody Response

Mozes

McDevitt

Jaton

et al. 1969

The Journal of Experimental Medicine

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The response of inbred mouse strains to two polypeptides derived from multichain polyprolines, (T,G)-Pro--L and (Phe,G)-Pro--L, is different from the response of the same mouse strains to a similar series of polymers built on multi-poly-D,L-alanyl--poly-L-lysine, although the same short sequences of amino acids are attached to the side chains of the polypeptides in the two series. These results indicate that a portion of the side chain (e.g. polyalanine or polyproline) participates in the antigenic determinant. This was confirmed by studying the response of different mouse strains to two kinds of polypeptides: (T,G)-Pro-A--L 717 and 718 and (T,G)-A-Pro--L 719 and 721. Antibody assay of antisera to (Phe,G)-Pro--L with the cross-reacting antigens (T,G)-Pro--L and (Phe,G)-A-L indicates that different inbred mouse strains make antibodies specific for different parts of the same polypeptide. Thus, antibody from DBA/1 mice reacts almost exclusively with the (Phe,G) sequence, while SJL antisera bind only (T,G)-Pro--L and fail to bind (Phe,G)-A-L. The immune responses to the same amino acids on two different polypeptides (i.e. A--L and Pro--L) appear to be under separate genetic control.

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Section: Ref 5)supporting

confidence: 71%

The Nature of the Antigenic Determinant in a Genetic Control of the Antibody Response

Mozes

McDevitt

Jaton

et al. 1969

The Journal of Experimental Medicine

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“…The almost 10 fold difference in antibody response to the same immunization schedule with GAT in the three sheep is probably a reflection of genetic differences as shown by M c D ev it t and Sela [14] and Maurer and Pinchuck [11] with this and other polymers in other species.…”

Section: Discussionmentioning

confidence: 98%

“…Anti-GAT sera from Swiss mice [11] showed cross-reactions of 100% or greater with GT, while the reaction with GA varied among individ ual animals from 0 to 35%. The antisera from inbred mouse strains showed a similar pattern of about 100% cross-reaction with GT and 0 to 40% with GA.…”

Section: Discussionmentioning

confidence: 99%

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Antigenicity of Polypeptides (Poly-α-Amino Acids)

Clark¹,

Maurer²

1969

Int Arch Allergy Immunol

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Genetics of the immune response. III. The restricted heterogeneity of antibodies to phage fd in a low responding inbred strain of mice

Kölsch

Diller

1971

Eur J Immunol

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induration is slight or absent. Reactions elicited by the protein conjugate (ABA GSA) are much stronger. On the other hand, with in vitro systems, ABA-tyrosine is as efficient as the protein conjugate.That an antigen could elicit an in vitro response (lymphocyte transformation) although not eliciting a cutaneous reaction, has also been reported for some oligo-lysines and DNP-lysines [ 1.51. It would therefore appear that, t o appreciate the immunogenicity of a substance of low molecular weight, it is not possible t o conclude that this substance cannot induce DH if it does not elicit a cutaneous reaction in the immunized animal. To detect a possible immunological response, it would be necessary either t o couple the antigenic determinant t o a protein, or t o examine cellular response in vitro..The difference in efficiency between ABA-tyrosine and ABA-GSA in the detection of DH in vivo appears at least partly linked t o the fact that the low molecular weight conjugate is cleared from the dermis far more rapidly than the protein conjugate (especially during the first hour after injection). Antigen clearance has been examined in unimmunized guinea pigs, for, according t o Eisen [ 161, the DH state does not alter the phenomenon.The immunochemical specificity of DH, induced by ABA. tyrosine$ under investigation. We would like t o thank Miss Odile Petit for her excellent technical assistance and Mrs. Anne Lecroisey for carrying out thin-layer chromatography.

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Immunogenicity of Synthetic Polymers of Amino Acids; Role of Carrier and Genetic Background

Cited by 7 publications

References 0 publications

The Nature of the Antigenic Determinant in a Genetic Control of the Antibody Response

The Nature of the Antigenic Determinant in a Genetic Control of the Antibody Response

Antigenicity of Polypeptides (Poly-α-Amino Acids)

Genetics of the immune response. III. The restricted heterogeneity of antibodies to phage fd in a low responding inbred strain of mice

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