Identification and Isolation of Surface-Exposed Portions of the Major Outer Membrane Protein ofChlamydia Trachomatisby Two-Dimensional Peptide Mapping and High-Performance Liquid Chromatography
- 1 July 1985
- journal article
- research article
- Published by Taylor & Francis in Journal of Liquid Chromatography
- Vol. 8 (9), 1559-1571
- https://doi.org/10.1080/01483918508074079
Abstract
In this study, we use high-performance liquid chromatography (HPLC) to isolate surface-peptides of the Chlamydia trachomatis serotype G major outer membrane protein (G-MOMP). The HPLC elution profile was compared with that of peptides of the G-MOMP which was iodinated with chloro-T. Two-dimensional peptide mapping of chloro-T 125I-labeled, surface-labeled peptides, and HPLC-isolated surface-peptides was then used to correlate HPLC-separated peptides with the 2-D maps of the G-MOMP. Results demonstrated that a 2-D-separated surface-peptide that had no apparent corresponding peptide in the 2-D chloro-T map was indeed present in the chloro-T labeled G-MOMP preparation, but at very low relative intensity, and that HPLC can be used to isolate surface-exposed regions of OM proteins for further immunological and structural studies.This publication has 12 references indexed in Scilit:
- 125I-Labeled Peptide Mapping and High-Performance Liquid Chromatography I-Peptide Separation of Protein I of Four Strains ofNeisseria GonorrhoeaeJournal of Liquid Chromatography, 1983
- Serology of Neisseria gonorrhoeae: coagglutination serogroups WI and WII/III correspond to different outer membrane protein I moleculesInfection and Immunity, 1982
- Surface peptide mapping of protein I and protein III of four strains of Neisseria gonorrhoeaeInfection and Immunity, 1982
- Monoclonal antibodies to Chlamydia trachomatis: antibody specificities and antigen characterization.The Journal of Immunology, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970