The University of Southampton
University of Southampton Institutional Repository

The major outer-membrane proteins of Chlamydia trachomatis serovars A and B: intra-serovar amino acid changes do not alter specificities of serovar- and C subspecies-reactive antibody-binding domains

The major outer-membrane proteins of Chlamydia trachomatis serovars A and B: intra-serovar amino acid changes do not alter specificities of serovar- and C subspecies-reactive antibody-binding domains
The major outer-membrane proteins of Chlamydia trachomatis serovars A and B: intra-serovar amino acid changes do not alter specificities of serovar- and C subspecies-reactive antibody-binding domains
The major outer-membrane protein (MOMP) of Chlamydia trachomatis is a promising candidate antigen for chlamydial vaccine development. We have sequenced the MOMP genes for a serovar A and a serovar B isolate and have compared these new sequences with those already reported. Intra-serovar changes in the inferred amino acid sequences of the surface-exposed variable segments known to be responsible for binding of neutralizing antibody were observed. Nevertheless, epitope mapping with solid-phase peptides showed that these intra-serovar changes did not affect the binding of serovar- and subspecies-specific, potentially protective antibodies. Variable segment 1 of C. trachomatis serovar A contained two adjacent antibody-binding sites, one of which was C-subspecies specific while the other was serovar A specific. Therefore the subspecies binding site for C-complex organisms is in variable segment 1, whilst that for B-complex organisms is in variable segment 4. This work shows that MOMP sequences are relatively stable within the serovar categorization for isolates taken decades apart from different continents. Within a given serovar, however, limited interchange of functionally related amino acids may occur without impairing the binding of serovar-specific antibody.
1350-0872
1559-1566
Hayes, L.J.
1bbf605d-315f-4099-beeb-f9ac2018e608
Pickett, M.A.
4b358cb6-2f2e-4691-a314-0e80df48eadb
Conlan, J.W.
80eceadc-14b1-481d-9812-14e7562d332f
Ferris, S.
3b0a8d88-429b-4379-8872-7d5ade3ffd54
Everson, J.S.
8f5e2cbc-b8f9-4ba6-9140-d726764d6c14
Ward, M.E.
a199bc96-75b6-415c-bffe-e68e8a00b468
Clarke, I.N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b
Hayes, L.J.
1bbf605d-315f-4099-beeb-f9ac2018e608
Pickett, M.A.
4b358cb6-2f2e-4691-a314-0e80df48eadb
Conlan, J.W.
80eceadc-14b1-481d-9812-14e7562d332f
Ferris, S.
3b0a8d88-429b-4379-8872-7d5ade3ffd54
Everson, J.S.
8f5e2cbc-b8f9-4ba6-9140-d726764d6c14
Ward, M.E.
a199bc96-75b6-415c-bffe-e68e8a00b468
Clarke, I.N.
ff6c9324-3547-4039-bb2c-10c0b3327a8b

Hayes, L.J., Pickett, M.A., Conlan, J.W., Ferris, S., Everson, J.S., Ward, M.E. and Clarke, I.N. (1990) The major outer-membrane proteins of Chlamydia trachomatis serovars A and B: intra-serovar amino acid changes do not alter specificities of serovar- and C subspecies-reactive antibody-binding domains. Microbiology, 136 (8), 1559-1566. (doi:10.1099/00221287-136-8-1559). (PMID:1702141)

Record type: Article

Abstract

The major outer-membrane protein (MOMP) of Chlamydia trachomatis is a promising candidate antigen for chlamydial vaccine development. We have sequenced the MOMP genes for a serovar A and a serovar B isolate and have compared these new sequences with those already reported. Intra-serovar changes in the inferred amino acid sequences of the surface-exposed variable segments known to be responsible for binding of neutralizing antibody were observed. Nevertheless, epitope mapping with solid-phase peptides showed that these intra-serovar changes did not affect the binding of serovar- and subspecies-specific, potentially protective antibodies. Variable segment 1 of C. trachomatis serovar A contained two adjacent antibody-binding sites, one of which was C-subspecies specific while the other was serovar A specific. Therefore the subspecies binding site for C-complex organisms is in variable segment 1, whilst that for B-complex organisms is in variable segment 4. This work shows that MOMP sequences are relatively stable within the serovar categorization for isolates taken decades apart from different continents. Within a given serovar, however, limited interchange of functionally related amino acids may occur without impairing the binding of serovar-specific antibody.

Full text not available from this repository.

More information

Published date: August 1990
Organisations: Faculty of Medicine

Identifiers

Local EPrints ID: 352633
URI: https://eprints.soton.ac.uk/id/eprint/352633
ISSN: 1350-0872
PURE UUID: de69531d-2291-4b9f-b7e1-7db552694b4a
ORCID for I.N. Clarke: ORCID iD orcid.org/0000-0002-4938-1620

Catalogue record

Date deposited: 04 Jun 2013 08:47
Last modified: 06 Jun 2018 13:19

Export record

Altmetrics

Contributors

Author: L.J. Hayes
Author: M.A. Pickett
Author: J.W. Conlan
Author: S. Ferris
Author: J.S. Everson
Author: M.E. Ward
Author: I.N. Clarke ORCID iD

University divisions

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 https://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.

×