Relation between optical configuration and immunogenicity of synthetic polypeptides

Borek, F.; Stupp, Yehudit; Fuchs, Sara; Sela, Michael

doi:10.1042/bj0960577

“…The same polymers, when made of L-amino acids (G4zL~A~0, G36I-~6Ts, G56 L3sTe), are effective antigens in rabbits, guinea pigs, mice, and humans and can carry haptene specificity for guinea pigs. Others have also shown that polymers of D-amino acids are non-immunogenic (15)(16)(17). These findings are compatible with our previous discussion (4,5), and the concept of others that the metabolism of the antigen (18,19), previous to the formation of the immunogenic fragment carrying the antigenic determinant, is a necessary but not sufficient cri-teflon for immunogenicity.…”

Section: Testing Of Sera--passive Cutaneous Anapkylaxis (Pca)supporting

confidence: 89%

Antigenicity of Polypeptides (Poly Alpha Amino Acids). X. Studies with Polymers of D Amino Acids.

Maurer

¹

1963

Experimental Biology and Medicine

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In continuation of studies to delineate some of the criteria for immunogenicity of synthetic random polymers of a-amino acids, we have investigated the contribution of the optical configuration of the amino acids. It was hoped that by studying the immunogenicity in several species of a variety of random terpolymers containing only D-a-amino acids or mixtures of D-and L-a-amino acids, some definite conclusions could be reached concerning the role of optical configuration in immunogenicity. Previously, we reported that two polymers consisting only of the D-a-amino acids, glutamic acid, alanine, and tyrosine (G60A40, G6oA30T10) 1 were not immunogenic in rabbits or guinea pigs (1), whereas the "isomeric" polymers of L-amino acids were effective immunogens (2, 3). Moreover, the polymer G60Aa0Ti0, made of I)-amino acids, could not act as a carrier in guinea pigs for the haptene specificity of arsanilic acid (4). The polymers employed in this study were optical variations of those previously shown to be immunogenic when made of L-a-amino acids. The findings on immunogenicity will be presented here and the immunochemical relationships of the polymers will be the subject of another publication. Materials and MethodsAntigens.--Random copolymers were prepared by the polymerization of the appropriate N-carboxy-a-amino acids anhydride of the configuration indicated in Table I, by methods referred to previously (1-5). The average molecular weights were obtained from viscosity measurements as well as from measurements with the analytical ultracentrifuge. 2 Some typica] sedimentation patterns of the preparations are shown in Fig. 1.

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“…The same polymers, when made of L-amino acids (G4zL~A~0, G36I-~6Ts, G56 L3sTe), are effective antigens in rabbits, guinea pigs, mice, and humans and can carry haptene specificity for guinea pigs. Others have also shown that polymers of D-amino acids are non-immunogenic (15)(16)(17). These findings are compatible with our previous discussion (4,5), and the concept of others that the metabolism of the antigen (18,19), previous to the formation of the immunogenic fragment carrying the antigenic determinant, is a necessary but not sufficient cri-teflon for immunogenicity.…”

Section: Discussionsupporting

confidence: 81%

Antigenicity of Polypeptides (Poly Alpha Amino Acids)

Maurer

¹

1965

The Journal of Experimental Medicine

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In continuation of studies to delineate some of the criteria for immunogenicity of synthetic random polymers of a-amino acids, we have investigated the contribution of the optical configuration of the amino acids. It was hoped that by studying the immunogenicity in several species of a variety of random terpolymers containing only D-a-amino acids or mixtures of D-and L-a-amino acids, some definite conclusions could be reached concerning the role of optical configuration in immunogenicity. Previously, we reported that two polymers consisting only of the D-a-amino acids, glutamic acid, alanine, and tyrosine (G60A40, G6oA30T10) 1 were not immunogenic in rabbits or guinea pigs (1), whereas the "isomeric" polymers of L-amino acids were effective immunogens (2, 3). Moreover, the polymer G60Aa0Ti0, made of I)-amino acids, could not act as a carrier in guinea pigs for the haptene specificity of arsanilic acid (4). The polymers employed in this study were optical variations of those previously shown to be immunogenic when made of L-a-amino acids. The findings on immunogenicity will be presented here and the immunochemical relationships of the polymers will be the subject of another publication. Materials and MethodsAntigens.--Random copolymers were prepared by the polymerization of the appropriate N-carboxy-a-amino acids anhydride of the configuration indicated in Table I, by methods referred to previously (1-5). The average molecular weights were obtained from viscosity measurements as well as from measurements with the analytical ultracentrifuge. 2 Some typica] sedimentation patterns of the preparations are shown in Fig. 1.

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“…It has been reported (Borek et al, 1967;Mannik and Stage, 1971) that specific antibodies can be isolated from antisera with the aid of immunoadsorbents. Immunoadsorbents of mitochondrial and nuclear GDH were prepared by binding either protein to CNBr-activated Sepharose.…”

Section: Resultsmentioning

confidence: 99%

Detection of structural differences between nuclear and mitochondrial glutamate dehydrogenases by the use of immunoadsorbents

Prisco¹,

Casola²

1975

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Structural differences between crystalline mitochondrial and nuclear glutamate dehydrogenases from ox liver have been detected by immunological techniques. Antisera prepared against each enzyme precipitate both glutamate dehydrogenases; upon immunodiffusion, the antiserum against the nuclear enzyme gives a line of incomplete identity with the two antigens, whereas the antiserum against the mitochondrial enzyme gives a line of complete identity. Fractionation of the antibodies contained in each antiserum by means of an immunoadsorbent, to which the nuclear or the mitochondrial enzyme has been covalently linked, shows that nuclear glutamate dehydrogenase (GDH) contains specific antigenic determinants as well as determinants common to the mitochondrial enzyme, whereas the latter appears to have no antigenic portions which are not present in the nuclear antigen, in accord with the results of immunodiffusion. The antibodies against determinants common to both enzymes precipitate and inhibit them, whereas the specific anti-nuclear GDH antibodies precipitate but do not inhibit the nuclear antigen.

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Relation between optical configuration and immunogenicity of synthetic polypeptides

Cited by 29 publications

References 13 publications

Antigenicity of Polypeptides (Poly Alpha Amino Acids). X. Studies with Polymers of D Amino Acids.

Antigenicity of Polypeptides (Poly Alpha Amino Acids). X. Studies with Polymers of D Amino Acids.

Antigenicity of Polypeptides (Poly Alpha Amino Acids)

Detection of structural differences between nuclear and mitochondrial glutamate dehydrogenases by the use of immunoadsorbents

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