The University of Southampton
University of Southampton Institutional Repository

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.

This record has no associated files available for download.

More information

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

Catalogue record

Date deposited: 03 Jun 2013 15:26
Last modified: 15 Mar 2024 02:33

Export record

Altmetrics

Contributors

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

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×