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Phage displayed 6-mer mimotopes with a consensus proline absent in the minimized linear wild-type epitope

Identifieur interne : 000198 ( Istex/Corpus ); précédent : 000197; suivant : 000199

Phage displayed 6-mer mimotopes with a consensus proline absent in the minimized linear wild-type epitope

Auteurs : Sabrina Deroo ; Philippe Fournier ; Dietmar Theisen ; Nicolas H. C. Brons ; Hans Deckmyn ; Claude P. Muller

Source :

RBID : ISTEX:D88406C219295F9B543D7A8FB2E4AA19AABEF3D5

English descriptors

Abstract

Abstract: Phage displayed random 6-mer libraries were screened with a monoclonal antibody specific for a minimized ‘linear’ 7-mer epitope of the measles virus hemagglutinin protein. No clone with the wild-type sequence was selected and most clones contained a sequence motif not found in the wild-type sequence. Two mimotopes (LYMPQLS, SEMPQLP) were synthesized which inhibited binding to the measles virus 95–135 times better than a wild-type peptide. Sequence comparison of proteins with known 3D-structure indicates that the epitope corresponds to an α-helix, while the best mimotopes have no predicted helix propensity. The proline is thought to be required for inducing a turn necessary for mimicking part of the α-helix. The higher intrinsic stability of such a mimotope may explain its improved binding and may be more suitable in immunogenicity experiments.

Url:
DOI: 10.1023/A:1008893218958

Links to Exploration step

ISTEX:D88406C219295F9B543D7A8FB2E4AA19AABEF3D5

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<Para>Phage displayed random 6-mer libraries were screened with a monoclonal antibody specific for a minimized ‘linear’ 7-mer epitope of the measles virus hemagglutinin protein. No clone with the wild-type sequence was selected and most clones contained a sequence motif not found in the wild-type sequence. Two mimotopes (LYMPQLS, SEMPQLP) were synthesized which inhibited binding to the measles virus 95–135 times better than a wild-type peptide. Sequence comparison of proteins with known 3D-structure indicates that the epitope corresponds to an α-helix, while the best mimotopes have no predicted helix propensity. The proline is thought to be required for inducing a turn necessary for mimicking part of the α-helix. The higher intrinsic stability of such a mimotope may explain its improved binding and may be more suitable in immunogenicity experiments.</Para>
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<abstract lang="en">Abstract: Phage displayed random 6-mer libraries were screened with a monoclonal antibody specific for a minimized ‘linear’ 7-mer epitope of the measles virus hemagglutinin protein. No clone with the wild-type sequence was selected and most clones contained a sequence motif not found in the wild-type sequence. Two mimotopes (LYMPQLS, SEMPQLP) were synthesized which inhibited binding to the measles virus 95–135 times better than a wild-type peptide. Sequence comparison of proteins with known 3D-structure indicates that the epitope corresponds to an α-helix, while the best mimotopes have no predicted helix propensity. The proline is thought to be required for inducing a turn necessary for mimicking part of the α-helix. The higher intrinsic stability of such a mimotope may explain its improved binding and may be more suitable in immunogenicity experiments.</abstract>
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