Sequence-simplification and chimeric assembly: New models of peptide antigen modification (385 views)
Mol Immunol (ISSN: 0161-5890), 2002 Nov; 39(7-8): 443-451.
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Paper type: Journal Article,
Impact factor: 2.414, 5-year impact factor: 2.897
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036842152&partnerID=40&md5=27effc578f7563a38fd1c0f40a22464e
Keywords: Antigen Modification, Chimeric Peptides, Molecular Surface, Simplified Peptides, Chimeric Antibody, Epitope, Glycine, Affinity Chromatography, Amino Acid Sequence, Amino Acid Substitution, Animal Experiment, Antibody Affinity, Antibody Production, Antibody Specificity, Antigen Antibody Reaction, Antigen Recognition, Article, Controlled Study, Cross Reaction, Enzyme Linked Immunosorbent Assay, Molecular Model, Nonhuman, Optical Biosensor, Priority Journal, Protein Assembly, Protein Modification, Synthesis, Antigen-Antibody Reactions, Enzyme-Linked Immunosorbent Assay, Kinetics, Molecular Sequence Data, Rabbits, Recombinant Fusion Proteins, Oryctolagus Cuniculus,
Affiliations:
*** IBB - CNR ***
TECNOGEN S.C.p.A., Parco Scientifico, 81015 Piana di Monte Verna (CE), Italy
TECNOGEN S. C. p. A., Parco Scientifico, 81015 Piana di Monte Verna (CE), Italy
References:
Bartnes, K., Hannestad, K., Guichard, G., Briand, J.P., A retro-inverso analog mimics the cognate peptide epitope of a CD4+ T-cell clone (1997) Eur. J. Immunol., 27, pp. 1387-139
Benkirane, N., Friede, M., Guichard, G., Briand, J.P., Van Regenmortel, M.H.V., Muller, S., Antigenicity and immunogenicity of modified synthetic peptides containing D-amino acid residues. Antibodies to a D-enantiomer do recognize the parent L-hexapeptide and reciprocally (1993) J. Biol. Chem., 268, pp. 26279-26285
Benkirane, N., Guichard, G., Van Regenmortel, H.H.V., Briand, J.P., Muller, S., Cross-reactivity of antibodies to retro-inverso peptidomimetics with the parent protein histone H3 and chromatin core particle. Specificity and kinetic rate-constant measurements (1995) J. Biol. Chem., 270, pp. 11921-11926
Borek, F., Stupp, Y., Fuchs, S., Sela, M., Relation between optical configuration and immunogenicity of synthetic polypeptides (1965) Biochem. J., 96, pp. 577-582
Briand, J.P., Guichard, G., Dumortier, H., Muller, S., Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases (1995) J. Biol. Chem., 270, pp. 20686-20691
Briand, J.P., Benkirane, N., Guichard, G., Newman, J.F., Van Regenmortel, M.H., Brown, F., Muller, S., A retro-inverso peptide corresponding to the GH loop of foot-and-mouth disease virus elicits high levels of long-lasting protective neutralizing antibodies (1997) Proc. Natl. Acad. Sci. U.S.A., 94, pp. 12545-12550
Brown, J.H., Jardetzky, T.S., Gorga, J.C., Stern, L.J., Urban, R.G., Strominger, J.L., Wiley, D.C., Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 (1993) Nature, 364, pp. 33-39
Collins, E.J., Garboczi, D.N., Wiley, D.C., Three-dimensional structure of a peptide extending from one end of a class I MHC binding site (1994) Nature, 371, pp. 626-629
Chorev, M., Goodman, M., Recent developments in retro peptides and proteins - An ongoing topochemical exploration (1995) Trends Biotechnol., 13, pp. 438-445
Dintzis, H.M., Symer, D.E., Dintzis, R.Z., Zawadzke, L.E., Berg, J.M., A comparison of the immunogenicity of a pair of enantiomeric proteins (1993) Proteins Struct. Funct. Genet., 16, pp. 306-308
Fassina, G., Cassani, G., Gnocchi, P., Fornasiero, M.C., Isetta, A.M., Inhibition of interleukin-2/p55 receptor subunit interaction by complementary peptides (1995) Arch. Biochem. Biophys., 318, pp. 37-54
Gill, T.J., Gould, J.H., Doty, P., Role of optical isomers in determining the antigenicity of synthetic polypeptides (1963) Nature, 197, pp. 746-747
Guichard, G., Benkirane, N., Graff, R., Muller, S., Briand, J.P., Synthesis and antigenic properties of reduced peptide bond pseudopeptide analogues of a histone H3 hexapeptide (1994) Pept. Res., 7, pp. 308-321
Higgins, K.A., Bicknell, W., Keach, H.H., Hearn, M.T., Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy (1997) J. Pept. Res., 50, pp. 421-435
Jameson, B.A., McDonnell, J.M., Marini, J.C., Korngold, R., A rationally designed CD4 analogue inhibits experimental allergic encephalomyelitis (1994) Nature, 368, pp. 744-746
Madden, D.R., Gorga, J.C., Strominger, J.L., Wiley, D.C., The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation (1991) Nature, 353, pp. 321-323
Marino, M., Ippolito, A., Ruvo, M., Scarallo, A., Volpe, S., Fassina, G., Prevention of experimental autoimmune encephalomyelitis by encephalitogenic epitope sequence simplified derivatives (2000) Mol. Immunol., 37, pp. 951-960
Maurer, P., Antigenicity of polypeptides (poly alpha amino acids) (1965) J. Exp. Med., 121, pp. 339-349
Meziere, C., Viguier, M., Dumortier, H., Lo-Man, R., Leclerc, C., Guillet, J.G., Briand, J.P., Muller, S., In vivo T helper cell response to retro-inverso peptidomimetics (1997) J. Immunol., 159, pp. 3230-3237
Muller, S., Guichard, G., Benkirane, N., Brown, F., Van Regenmortel, M.H.V., Briand, J.P., Enhanced immunogenicity and cross-reactivity of retro-inverso peptidomimetics of the major antigenic site of foot-and-mouth disease virus (1995) Pept. Res., 8, pp. 138-144
Ostankovitch, M., Guichard, G., Connan, F., Muller, S., Chaboissier, A., Hoebeke, J., Choppin, J., Guillet, J.G., A partially modified retro-inverso pseudopeptide modulates the cytokine profile of CTL specific for an influenza virus epitope (1998) J. Immunol., 161, pp. 200-208
Petit, M.C., Benkirane, N., Guichard, G., Du, A.P., Marraud, M., Cung, M.T., Briand, J.P., Muller, S., Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide (1999) J. Biol. Chem., 274, pp. 3686-3692
Phan-Chan-Du, A., Petit, M.C., Guichard, G., Briand, J.P., Muller, S., Cung, M.T., Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach (2001) Biochemistry, 40, pp. 5720-5727
Rini, J.M., Schulze-Gahmen, U., Wilson, I.A., Structural evidence for induced fit as a mechanism for antibody-antigen recognition (1992) Science, 255, pp. 959-965
Rini, J.M., Stanfield, R.L., Stura, E.A., Salinas, P.A., Profy, A.T., Wilson, I.A., Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen (1993) Proc. Natl. Acad. Sci. U.S.A., 90, pp. 6325-6329
Shoham, M., Crystal structure of anticholera toxin peptide complex at 2.3 Å (1993) J. Mol. Biol., 232, pp. 1169-1175
Siligardi, G., Drake, A.F., The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides (1995) Biopolymers (Pep. Sci.), 37, pp. 281-292
Srinivasan, M., Wardrop, R.M., Gienapp, I.E., Stuckman, S.S., Whitacre, C.C., Kaumaya, P.T., A retro-inverso peptide mimic of CD28 encompassing the MYPPPY motif adopts a polyproline type II helix and inhibits encephalitogenic T cells in vitro (2001) J. Immunol., 167, pp. 578-585
Stebbins, C.E., Galan, J.E., Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion (2001) Nature, 414, pp. 77-81
Taylor, E.M., Otero, D.A., Banks, W.A., O'Brien, J.S., Retro-inverso prosaptide peptides retain bioactivity, are stable in vivo, are blood-brain barrier permeable (2000) J. Pharmacol. Exp. Ther., 295, pp. 190-194
Verdoliva, A., Cassani, G., Fassina, G., Affinity purification of polyclonal antibodies using immobilized multimeric peptides (1995) J. Chromatogr. Biomed. Appl., 664, pp. 175-183
Verdoliva, A., Ruvo, M., Cassani, G., Fassina, G., Antigenicity of topochemically related peptides (1995) Biochem. Biophys. Acta, 1253, pp. 57-62
Briand, J. P., Guichard, G., Dumortier, H., Muller, S., Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases (1995) J. Biol. Chem., 270, pp. 20686-20691
Briand, J. P., Benkirane, N., Guichard, G., Newman, J. F., Van Regenmortel, M. H., Brown, F., Muller, S., A retro-inverso peptide corresponding to the GH loop of foot-and-mouth disease virus elicits high levels of long-lasting protective neutralizing antibodies (1997) Proc. Natl. Acad. Sci. U. S. A., 94, pp. 12545-12550
Brown, J. H., Jardetzky, T. S., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L., Wiley, D. C., Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 (1993) Nature, 364, pp. 33-39
Collins, E. J., Garboczi, D. N., Wiley, D. C., Three-dimensional structure of a peptide extending from one end of a class I MHC binding site (1994) Nature, 371, pp. 626-629
Dintzis, H. M., Symer, D. E., Dintzis, R. Z., Zawadzke, L. E., Berg, J. M., A comparison of the immunogenicity of a pair of enantiomeric proteins (1993) Proteins Struct. Funct. Genet., 16, pp. 306-308
Gill, T. J., Gould, J. H., Doty, P., Role of optical isomers in determining the antigenicity of synthetic polypeptides (1963) Nature, 197, pp. 746-747
Higgins, K. A., Bicknell, W., Keach, H. H., Hearn, M. T., Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy (1997) J. Pept. Res., 50, pp. 421-435
Jameson, B. A., McDonnell, J. M., Marini, J. C., Korngold, R., A rationally designed CD4 analogue inhibits experimental allergic encephalomyelitis (1994) Nature, 368, pp. 744-746
Madden, D. R., Gorga, J. C., Strominger, J. L., Wiley, D. C., The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation (1991) Nature, 353, pp. 321-323
Petit, M. C., Benkirane, N., Guichard, G., Du, A. P., Marraud, M., Cung, M. T., Briand, J. P., Muller, S., Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide (1999) J. Biol. Chem., 274, pp. 3686-3692
Rini, J. M., Schulze-Gahmen, U., Wilson, I. A., Structural evidence for induced fit as a mechanism for antibody-antigen recognition (1992) Science, 255, pp. 959-965
Rini, J. M., Stanfield, R. L., Stura, E. A., Salinas, P. A., Profy, A. T., Wilson, I. A., Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50. 1, in complex with its V3 loop peptide antigen (1993) Proc. Natl. Acad. Sci. U. S. A., 90, pp. 6325-6329
Stebbins, C. E., Galan, J. E., Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion (2001) Nature, 414, pp. 77-81
Taylor, E. M., Otero, D. A., Banks, W. A., O'Brien, J. S., Retro-inverso prosaptide peptides retain bioactivity, are stable in vivo, are blood-brain barrier permeable (2000) J. Pharmacol. Exp. Ther., 295, pp. 190-194
Mol Immunol (ISSN: 0161-5890), 2002 Nov; 39(7-8): 443-451.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.414, 5-year impact factor: 2.897
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036842152&partnerID=40&md5=27effc578f7563a38fd1c0f40a22464e
Keywords: Antigen Modification, Chimeric Peptides, Molecular Surface, Simplified Peptides, Chimeric Antibody, Epitope, Glycine, Affinity Chromatography, Amino Acid Sequence, Amino Acid Substitution, Animal Experiment, Antibody Affinity, Antibody Production, Antibody Specificity, Antigen Antibody Reaction, Antigen Recognition, Article, Controlled Study, Cross Reaction, Enzyme Linked Immunosorbent Assay, Molecular Model, Nonhuman, Optical Biosensor, Priority Journal, Protein Assembly, Protein Modification, Synthesis, Antigen-Antibody Reactions, Enzyme-Linked Immunosorbent Assay, Kinetics, Molecular Sequence Data, Rabbits, Recombinant Fusion Proteins, Oryctolagus Cuniculus,
Affiliations:
*** IBB - CNR ***
TECNOGEN S.C.p.A., Parco Scientifico, 81015 Piana di Monte Verna (CE), Italy
TECNOGEN S. C. p. A., Parco Scientifico, 81015 Piana di Monte Verna (CE), Italy
References:
Bartnes, K., Hannestad, K., Guichard, G., Briand, J.P., A retro-inverso analog mimics the cognate peptide epitope of a CD4+ T-cell clone (1997) Eur. J. Immunol., 27, pp. 1387-139
Benkirane, N., Friede, M., Guichard, G., Briand, J.P., Van Regenmortel, M.H.V., Muller, S., Antigenicity and immunogenicity of modified synthetic peptides containing D-amino acid residues. Antibodies to a D-enantiomer do recognize the parent L-hexapeptide and reciprocally (1993) J. Biol. Chem., 268, pp. 26279-26285
Benkirane, N., Guichard, G., Van Regenmortel, H.H.V., Briand, J.P., Muller, S., Cross-reactivity of antibodies to retro-inverso peptidomimetics with the parent protein histone H3 and chromatin core particle. Specificity and kinetic rate-constant measurements (1995) J. Biol. Chem., 270, pp. 11921-11926
Borek, F., Stupp, Y., Fuchs, S., Sela, M., Relation between optical configuration and immunogenicity of synthetic polypeptides (1965) Biochem. J., 96, pp. 577-582
Briand, J.P., Guichard, G., Dumortier, H., Muller, S., Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases (1995) J. Biol. Chem., 270, pp. 20686-20691
Briand, J.P., Benkirane, N., Guichard, G., Newman, J.F., Van Regenmortel, M.H., Brown, F., Muller, S., A retro-inverso peptide corresponding to the GH loop of foot-and-mouth disease virus elicits high levels of long-lasting protective neutralizing antibodies (1997) Proc. Natl. Acad. Sci. U.S.A., 94, pp. 12545-12550
Brown, J.H., Jardetzky, T.S., Gorga, J.C., Stern, L.J., Urban, R.G., Strominger, J.L., Wiley, D.C., Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 (1993) Nature, 364, pp. 33-39
Collins, E.J., Garboczi, D.N., Wiley, D.C., Three-dimensional structure of a peptide extending from one end of a class I MHC binding site (1994) Nature, 371, pp. 626-629
Chorev, M., Goodman, M., Recent developments in retro peptides and proteins - An ongoing topochemical exploration (1995) Trends Biotechnol., 13, pp. 438-445
Dintzis, H.M., Symer, D.E., Dintzis, R.Z., Zawadzke, L.E., Berg, J.M., A comparison of the immunogenicity of a pair of enantiomeric proteins (1993) Proteins Struct. Funct. Genet., 16, pp. 306-308
Fassina, G., Cassani, G., Gnocchi, P., Fornasiero, M.C., Isetta, A.M., Inhibition of interleukin-2/p55 receptor subunit interaction by complementary peptides (1995) Arch. Biochem. Biophys., 318, pp. 37-54
Gill, T.J., Gould, J.H., Doty, P., Role of optical isomers in determining the antigenicity of synthetic polypeptides (1963) Nature, 197, pp. 746-747
Guichard, G., Benkirane, N., Graff, R., Muller, S., Briand, J.P., Synthesis and antigenic properties of reduced peptide bond pseudopeptide analogues of a histone H3 hexapeptide (1994) Pept. Res., 7, pp. 308-321
Higgins, K.A., Bicknell, W., Keach, H.H., Hearn, M.T., Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy (1997) J. Pept. Res., 50, pp. 421-435
Jameson, B.A., McDonnell, J.M., Marini, J.C., Korngold, R., A rationally designed CD4 analogue inhibits experimental allergic encephalomyelitis (1994) Nature, 368, pp. 744-746
Madden, D.R., Gorga, J.C., Strominger, J.L., Wiley, D.C., The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation (1991) Nature, 353, pp. 321-323
Marino, M., Ippolito, A., Ruvo, M., Scarallo, A., Volpe, S., Fassina, G., Prevention of experimental autoimmune encephalomyelitis by encephalitogenic epitope sequence simplified derivatives (2000) Mol. Immunol., 37, pp. 951-960
Maurer, P., Antigenicity of polypeptides (poly alpha amino acids) (1965) J. Exp. Med., 121, pp. 339-349
Meziere, C., Viguier, M., Dumortier, H., Lo-Man, R., Leclerc, C., Guillet, J.G., Briand, J.P., Muller, S., In vivo T helper cell response to retro-inverso peptidomimetics (1997) J. Immunol., 159, pp. 3230-3237
Muller, S., Guichard, G., Benkirane, N., Brown, F., Van Regenmortel, M.H.V., Briand, J.P., Enhanced immunogenicity and cross-reactivity of retro-inverso peptidomimetics of the major antigenic site of foot-and-mouth disease virus (1995) Pept. Res., 8, pp. 138-144
Ostankovitch, M., Guichard, G., Connan, F., Muller, S., Chaboissier, A., Hoebeke, J., Choppin, J., Guillet, J.G., A partially modified retro-inverso pseudopeptide modulates the cytokine profile of CTL specific for an influenza virus epitope (1998) J. Immunol., 161, pp. 200-208
Petit, M.C., Benkirane, N., Guichard, G., Du, A.P., Marraud, M., Cung, M.T., Briand, J.P., Muller, S., Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide (1999) J. Biol. Chem., 274, pp. 3686-3692
Phan-Chan-Du, A., Petit, M.C., Guichard, G., Briand, J.P., Muller, S., Cung, M.T., Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach (2001) Biochemistry, 40, pp. 5720-5727
Rini, J.M., Schulze-Gahmen, U., Wilson, I.A., Structural evidence for induced fit as a mechanism for antibody-antigen recognition (1992) Science, 255, pp. 959-965
Rini, J.M., Stanfield, R.L., Stura, E.A., Salinas, P.A., Profy, A.T., Wilson, I.A., Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen (1993) Proc. Natl. Acad. Sci. U.S.A., 90, pp. 6325-6329
Shoham, M., Crystal structure of anticholera toxin peptide complex at 2.3 Å (1993) J. Mol. Biol., 232, pp. 1169-1175
Siligardi, G., Drake, A.F., The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides (1995) Biopolymers (Pep. Sci.), 37, pp. 281-292
Srinivasan, M., Wardrop, R.M., Gienapp, I.E., Stuckman, S.S., Whitacre, C.C., Kaumaya, P.T., A retro-inverso peptide mimic of CD28 encompassing the MYPPPY motif adopts a polyproline type II helix and inhibits encephalitogenic T cells in vitro (2001) J. Immunol., 167, pp. 578-585
Stebbins, C.E., Galan, J.E., Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion (2001) Nature, 414, pp. 77-81
Taylor, E.M., Otero, D.A., Banks, W.A., O'Brien, J.S., Retro-inverso prosaptide peptides retain bioactivity, are stable in vivo, are blood-brain barrier permeable (2000) J. Pharmacol. Exp. Ther., 295, pp. 190-194
Verdoliva, A., Cassani, G., Fassina, G., Affinity purification of polyclonal antibodies using immobilized multimeric peptides (1995) J. Chromatogr. Biomed. Appl., 664, pp. 175-183
Verdoliva, A., Ruvo, M., Cassani, G., Fassina, G., Antigenicity of topochemically related peptides (1995) Biochem. Biophys. Acta, 1253, pp. 57-62
Briand, J. P., Guichard, G., Dumortier, H., Muller, S., Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases (1995) J. Biol. Chem., 270, pp. 20686-20691
Briand, J. P., Benkirane, N., Guichard, G., Newman, J. F., Van Regenmortel, M. H., Brown, F., Muller, S., A retro-inverso peptide corresponding to the GH loop of foot-and-mouth disease virus elicits high levels of long-lasting protective neutralizing antibodies (1997) Proc. Natl. Acad. Sci. U. S. A., 94, pp. 12545-12550
Brown, J. H., Jardetzky, T. S., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L., Wiley, D. C., Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 (1993) Nature, 364, pp. 33-39
Collins, E. J., Garboczi, D. N., Wiley, D. C., Three-dimensional structure of a peptide extending from one end of a class I MHC binding site (1994) Nature, 371, pp. 626-629
Dintzis, H. M., Symer, D. E., Dintzis, R. Z., Zawadzke, L. E., Berg, J. M., A comparison of the immunogenicity of a pair of enantiomeric proteins (1993) Proteins Struct. Funct. Genet., 16, pp. 306-308
Gill, T. J., Gould, J. H., Doty, P., Role of optical isomers in determining the antigenicity of synthetic polypeptides (1963) Nature, 197, pp. 746-747
Higgins, K. A., Bicknell, W., Keach, H. H., Hearn, M. T., Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy (1997) J. Pept. Res., 50, pp. 421-435
Jameson, B. A., McDonnell, J. M., Marini, J. C., Korngold, R., A rationally designed CD4 analogue inhibits experimental allergic encephalomyelitis (1994) Nature, 368, pp. 744-746
Madden, D. R., Gorga, J. C., Strominger, J. L., Wiley, D. C., The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation (1991) Nature, 353, pp. 321-323
Petit, M. C., Benkirane, N., Guichard, G., Du, A. P., Marraud, M., Cung, M. T., Briand, J. P., Muller, S., Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide (1999) J. Biol. Chem., 274, pp. 3686-3692
Rini, J. M., Schulze-Gahmen, U., Wilson, I. A., Structural evidence for induced fit as a mechanism for antibody-antigen recognition (1992) Science, 255, pp. 959-965
Rini, J. M., Stanfield, R. L., Stura, E. A., Salinas, P. A., Profy, A. T., Wilson, I. A., Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50. 1, in complex with its V3 loop peptide antigen (1993) Proc. Natl. Acad. Sci. U. S. A., 90, pp. 6325-6329
Stebbins, C. E., Galan, J. E., Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion (2001) Nature, 414, pp. 77-81
Taylor, E. M., Otero, D. A., Banks, W. A., O'Brien, J. S., Retro-inverso prosaptide peptides retain bioactivity, are stable in vivo, are blood-brain barrier permeable (2000) J. Pharmacol. Exp. Ther., 295, pp. 190-194
Sequence-simplification and chimeric assembly: New models of peptide antigen modification
Sequence-simplified variants of a 15-mer peptide antigen, identified by amino acid side chains in alternating positions were synthesized introducing glycine residues alternatively in the parent peptide sequence and used to induce antibodies in rabbit. They reacted to a significant extent with anti-parent peptide antibodies, and in addition, affinity purified antibodies against these halved forms recognized with similar affinity and specificity, the starting peptide in affinity chromatography, optical biosensor and enzyme linked immunosorbent assay (ELISA) experiments, while no cross-reactivity was detected between reduced antigens. These findings suggest that a peptide antigen can display two molecular surfaces of recognition, identified by side chains of residues in alternating positions. Each surface can even take part in antigen/antibody interaction independently, thus indicating the possibility to select and assembly sequence-simplified forms belonging to different epitopes, also deriving from different molecules, to generate new structures incorporating a two-fold antigen/antibody specificity. Two "chimeric" forms were then synthesized starting from the P15 and P13 complementary peptides, both able to bind interleukin 2. These structures, showing simultaneously trans-surfaces of recognition belonging to both parent forms, have been found to retain antigenic properties against antibodies of simplified P15 derivatives showing the same molecular surface of recognition. In addition, anti-chimeric antibodies recognized both P15 and P13 starting peptides, while no cross-antibody recognition was observed between chimeric antigens. © 2002 Elsevier Science Ltd. All rights reserved.
Sequence-simplified variants of a 15-mer peptide antigen, identified by amino acid side chains in alternating positions were synthesized introducing glycine residues alternatively in the parent peptide sequence and used to induce antibodies in rabbit. They reacted to a significant extent with anti-parent peptide antibodies, and in addition, affinity purified antibodies against these halved forms recognized with similar affinity and specificity, the starting peptide in affinity chromatography, optical biosensor and enzyme linked immunosorbent assay (ELISA) experiments, while no cross-reactivity was detected between reduced antigens. These findings suggest that a peptide antigen can display two molecular surfaces of recognition, identified by side chains of residues in alternating positions. Each surface can even take part in antigen/antibody interaction independently, thus indicating the possibility to select and assembly sequence-simplified forms belonging to different epitopes, also deriving from different molecules, to generate new structures incorporating a two-fold antigen/antibody specificity. Two "chimeric" forms were then synthesized starting from the P15 and P13 complementary peptides, both able to bind interleukin 2. These structures, showing simultaneously trans-surfaces of recognition belonging to both parent forms, have been found to retain antigenic properties against antibodies of simplified P15 derivatives showing the same molecular surface of recognition. In addition, anti-chimeric antibodies recognized both P15 and P13 starting peptides, while no cross-antibody recognition was observed between chimeric antigens. © 2002 Elsevier Science Ltd. All rights reserved.
Sequence-simplification and chimeric assembly: New models of peptide antigen modification
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