MersV1, Main, Exploration, bibRecord, 003B35

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

Identifieur interne : 003B35 ( Main/Exploration ); précédent : 003B34; suivant : 003B36

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

Auteurs : Sabrina Deroo [Luxembourg (pays)] ; Philippe Fournier [Luxembourg (pays)] ; Dietmar Theisen [Luxembourg (pays)] ; Nicolas H. C. Brons [Luxembourg (pays)] ; Hans Deckmyn [Belgique] ; Claude P. Muller [Luxembourg (pays)]

Source :

Letters in Peptide Science [ 0929-5666 ] ; 1998-05-01.

RBID : ISTEX:CBAE66D457E6A1AA54EE971058B312F46AE613BA

English descriptors

KwdEn :
- measles virus, monoclonal antibody, peptides, phage display libraries.

Abstract

Summary: 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 neccesary 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: 10.1007/BF02443461

Affiliations:

Belgique, Luxembourg (pays)

Le document en format XML

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<front><div type="abstract" xml:lang="en">Summary: 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 neccesary 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.</div>
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Serveur d'exploration MERS

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

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

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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