Cysteine-rich outer membrane proteins of Chlamydia trachomatis display compensatory sequence changes between biovariants

Mol Microbiol. 1990 Sep;4(9):1543-50. doi: 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 58,000 (outer membrane protein 2; OMP2) and 15,000 (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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / genetics*
  • Base Sequence
  • Chlamydia trachomatis / genetics*
  • Chlamydia trachomatis / metabolism
  • Cysteine
  • Genes, Bacterial
  • Genetic Variation*
  • Immunoblotting
  • Molecular Sequence Data
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • Bacterial Outer Membrane Proteins
  • Omp2 protein, bacteria
  • Cysteine

Associated data

  • GENBANK/X54450
  • GENBANK/X54451