Cysteine‐rich outer membrane proteins of Chlamydia trachomatis display compensatory sequence changes between biovariants
- 1 September 1990
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 4 (9) , 1543-1550
- https://doi.org/10.1111/j.1365-2958.1990.tb02065.x
Abstract
Two cysteine‐rich proteins of Chlamydia trachomatis are essential structural components of the unique outer membrane of the infectious elementary body. These 58000 (outer membrane protein 2; OMP2) and 15000 (OMP3) proteins also differ structurally and chemically between biovariants that differ in invasive capability. We have identified the gene for OMP3 and sequenced both trachoma and lymphogranuloma venereum (LGV) omp3 genes. We have previously sequenced omp2 from the LGV biovar and now describe the omp2 sequence for a trachoma biovariant. Amino acid sequence differences between biovariants were few but, significantly, these changes have altered the charge of both OMP2 and OMP3 such that the net charge of each protein differs between biovariants. These compensatory charge alterations have implications for the outer membrane organization of these proteins. In addition, examination of the OMP3 sequence suggests that OMP3 may be a lipoprotein.Keywords
This publication has 35 references indexed in Scilit:
- The structure of signal peptides from bacterial lipoproteinsProtein Engineering, Design and Selection, 1989
- Molecular cloning and sequence analysis of a developmentally regulated cysteine-rich outer membrane protein from Chlamydia trachomatisGene, 1988
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- Distinctive properties of signal sequences from bacterial lipoproteinsProtein Engineering, Design and Selection, 1988
- Signal sequencesJournal of Molecular Biology, 1985
- Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coliMolecular and Cellular Biochemistry, 1984
- Patterns of Amino Acids near Signal‐Sequence Cleavage SitesEuropean Journal of Biochemistry, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Conformational preferences of amino acids in globular proteinsBiochemistry, 1978
- A Search for the Bacterial Mucopeptide Component, Muramic Acid, in ChlamydiaJournal of General Microbiology, 1974