Expression of two novel proteins in Chlamydia trachomatis during natural infection
- Publication Type:
- Journal Article
- Citation:
- Microbial Pathogenesis, 2000, 29 (2), pp. 63 - 72
- Issue Date:
- 2000-01-01
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Genes for a putative membrane associated protein (mvi-homologue) and a 48 kDa protein (ctr48) in Chlamydia trachomatis were characterized. The mvi-homologue has 12 transmembrane domains and shows considerable homology to the members of this gene family in various organisms. The ctr48 has a leader sequence and the C-proximal half is tryptophan-rich. The latter region shares 65% identity with the N-proxima third of C. pneumoniae 76 kDa protein over an overlap of 231 amino acid residues. The genes for the mvi-homologue and the ctr48 are present in the B, Ba, D, E, J and L2 serotypes of C. trachomatis. Immediately downstream from the ctr48 gene are multiple stop codons which are followed by a functional rho-independent terminator. The mvi-homologue and ctr48 genes are independently transcribed, albeit poorly in serotype B. However, protein products corresponding to these genes could not be detected by western blotting in HEp2 cells infected with C. trachomatis. Nevertheless, antibodies to peptides corresponding to these proteins were detected in sera with high micro-immunofluorescence titre against C. trachomatic, collected from a Chlamydia-endemic population. These results suggest that the mvi-homologue and ctr48 are expressed by C. trachomatis during natural infection. (C) 2000 Academic Press.
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