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Cysteine‐rich outer membrane proteins of Chlamydia trachomatis display compensatory sequence changes between biovariants
Author(s) -
Allen J. E.,
Cerrone M. C.,
Beatty P. R.,
Stephens R. S.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb02065.x
Subject(s) - biology , chlamydia trachomatis , bacterial outer membrane , lymphogranuloma venereum , chlamydiaceae , peptide sequence , trachoma , membrane protein , gene , chlamydiales , genetics , microbiology and biotechnology , virology , escherichia coli , membrane , medicine , pathology
Summary 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.