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The major outer membrane protein of Chlamydia trachomatis: critical binding site and conformation determine the specificity of antibody binding to viable chlamydiae

The major outer membrane protein of Chlamydia trachomatis: critical binding site and conformation determine the specificity of antibody binding to viable chlamydiae
The major outer membrane protein of Chlamydia trachomatis: critical binding site and conformation determine the specificity of antibody binding to viable chlamydiae
The major outer membrane protein (MOMP) is the prime candidate for the development of a chlamydial vaccine. Antibodies to the subspecies-specific epitope neutralize chlamydial infection. Monoclonal antibodies (MAbs) to this epitope were prepared either by immunization with whole chlamydiae or with a 16 amino acid synthetic peptide. The critical binding site on the subspecies epitope for these MAbs was determined to single amino acid resolution using several hundred solid-phase peptides. A frame shift of just one amino acid in critical binding site completely prevented antibody binding to viable chlamydiae. A single MAb to whole organisms was capable of spanning both the surface-exposed, conformation-dependent, subspecies epitope and a buried, conformation-independent species epitope some 10 A distant. Immunization with peptide generated an MAb with reduced binding constraints which permitted the antibody to bind with broadened species-specificity at the subspecies binding site. The results show for the first time the importance of both critical binding site and conformation at the subspecies epitope. We suggest that the conformational flexibility of short, epitopic peptide vaccines may in some cases be advantageous, giving rise to extended specificity not attained with the natural protein.
0950-382X
311-318
Conlan, J.W.
80eceadc-14b1-481d-9812-14e7562d332f
Kajbaf, M.
f8979b2f-5797-4463-9545-7d7741b78de8
Clarke, I.N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Chantler, S.
4b3ef9ce-d787-45f3-abab-14716b96e06c
Ward, M.E.
a199bc96-75b6-415c-bffe-e68e8a00b468
Conlan, J.W.
80eceadc-14b1-481d-9812-14e7562d332f
Kajbaf, M.
f8979b2f-5797-4463-9545-7d7741b78de8
Clarke, I.N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Chantler, S.
4b3ef9ce-d787-45f3-abab-14716b96e06c
Ward, M.E.
a199bc96-75b6-415c-bffe-e68e8a00b468

Conlan, J.W., Kajbaf, M., Clarke, I.N., Chantler, S. and Ward, M.E. (1989) The major outer membrane protein of Chlamydia trachomatis: critical binding site and conformation determine the specificity of antibody binding to viable chlamydiae. Molecular Microbiology, 3 (3), 311-318. (doi:10.1111/j.1365-2958.1989.tb00176.x). (PMID:2473372)

Record type: Article

Abstract

The major outer membrane protein (MOMP) is the prime candidate for the development of a chlamydial vaccine. Antibodies to the subspecies-specific epitope neutralize chlamydial infection. Monoclonal antibodies (MAbs) to this epitope were prepared either by immunization with whole chlamydiae or with a 16 amino acid synthetic peptide. The critical binding site on the subspecies epitope for these MAbs was determined to single amino acid resolution using several hundred solid-phase peptides. A frame shift of just one amino acid in critical binding site completely prevented antibody binding to viable chlamydiae. A single MAb to whole organisms was capable of spanning both the surface-exposed, conformation-dependent, subspecies epitope and a buried, conformation-independent species epitope some 10 A distant. Immunization with peptide generated an MAb with reduced binding constraints which permitted the antibody to bind with broadened species-specificity at the subspecies binding site. The results show for the first time the importance of both critical binding site and conformation at the subspecies epitope. We suggest that the conformational flexibility of short, epitopic peptide vaccines may in some cases be advantageous, giving rise to extended specificity not attained with the natural protein.

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Published date: March 1989
Organisations: Faculty of Medicine

Identifiers

Local EPrints ID: 352627
URI: http://eprints.soton.ac.uk/id/eprint/352627
ISSN: 0950-382X
PURE UUID: b055489e-b50d-453c-aee5-fdcd078a89c5
ORCID for I.N. Clarke: ORCID iD orcid.org/0000-0002-4938-1620

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Date deposited: 03 Jun 2013 15:26
Last modified: 18 Feb 2021 16:32

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Contributors

Author: J.W. Conlan
Author: M. Kajbaf
Author: I.N. Clarke ORCID iD
Author: S. Chantler
Author: M.E. Ward

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