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

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

doi:10.1007/BF02443461

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

Sabrina Deroo, Philippe Fournier, Dietmar Theisen, Nicolas H.C. Brons, Hans Deckmyn, Claude P. Muller^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Research › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	159-162
Number of pages	4
Journal	Letters in Peptide Science
Volume	5
Issue number	2-3
DOIs	https://doi.org/10.1007/BF02443461
Publication status	Published - 1998

Keywords

Measles virus
Monoclonal antibody
Peptides
Phage display libraries

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10.1007/BF02443461

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

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.",

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author = "Sabrina Deroo and Philippe Fournier and Dietmar Theisen and Brons, {Nicolas H.C.} and Hans Deckmyn and Muller, {Claude P.}",

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T1 - Phage displayed 6-mer mimotopes with a consensus proline absent in the minimized linear wild-type epitope

AU - Deroo, Sabrina

AU - Fournier, Philippe

AU - Theisen, Dietmar

AU - Brons, Nicolas H.C.

AU - Deckmyn, Hans

AU - Muller, Claude P.

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

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KW - Peptides

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

Abstract

Keywords

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