Mapping antigenic sites on the major outer membrane protein of Chlamydia trachomatis with synthetic peptides

Guangming Zhong, R. E. Reid, R. C. Brunham

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

The antigenicity of the major outer membrane protein (MOMP) of Chlamydia trachomatis was comprehensively evaluated by using overlapping hexapeptide homologs of serovar B MOMP and polyclonal rabbit antisera in a peptide enzyme-linked immunosorbent assay. Of 367 hexapeptides, 152 showed reactivities with at least one antiserum. Seven hexapeptides located within variable domain (VD) IV (residues 288 to 316) were found to be most reactive in terms of their binding titer and frequency, suggesting that VD IV is the immunodominant region within the MOMP as detected by this assay. Peptide-reactive antibodies could also recognize corresponding epitopes on either viable oracetone-permeabilized organisms. The antigenic specificity and immunoaccessibility of epitopes located in VD IV were resolved by absorbing antisera with chlamydial elementary bodies. Six antigenic sites were found in this region and included a B-type-specific site (S1), four subserogroup-specific sites (S2 and S4 to 6), and one species-specific site (S3), each displaying varying degrees of surface exposures on elementary bodies from different C. trachomatis serovars.

Original languageEnglish (US)
Pages (from-to)1450-1455
Number of pages6
JournalInfection and Immunity
Volume58
Issue number5
StatePublished - 1990
Externally publishedYes

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Immune Sera
Epitopes
Peptides
Membrane Proteins
Immunodominant Epitopes
Chlamydia trachomatis
Enzyme-Linked Immunosorbent Assay
Rabbits
Antibodies
Chlamydia trachomatis omp1 protein
Serogroup

ASJC Scopus subject areas

  • Immunology

Cite this

Mapping antigenic sites on the major outer membrane protein of Chlamydia trachomatis with synthetic peptides. / Zhong, Guangming; Reid, R. E.; Brunham, R. C.

In: Infection and Immunity, Vol. 58, No. 5, 1990, p. 1450-1455.

Research output: Contribution to journalArticle

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