Sequence-simplification and chimeric assembly: New models of peptide antigen modification (613 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:
Not available.
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:
Not available.
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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