Schmiel D H, Raulston J E, Fox E, Wyrick P B
Department of Microbiology and Immunology, University of North Carolina School of Medicine, Chapel Hill 27599, USA.
Microb Pathog. 1995 Oct;19(4):227-36. doi: 10.1016/s0882-4010(95)90281-3.
Genital serovariants of Chlamydia trachomatis establish infection by attachment, entry and multiplication within human endometrial epithelial cells. In previous studies, a chlamydial recombinant Escherichia coli was identified which exhibited a specific adherent phenotype to endometrial epithelial cells closely resembling that observed for a genital strain of C. trachomatis. One of the plasmid-encoded products expressed by the recombinant is a 28 kDa protein. In this study, localization of the 28 kDa protein in isolated outer membranes of recombinant E. coli and in chlamydial outer membrane complexes lends support for a potential role for this protein in the attachment process. Surprisingly, nucleic acid sequence analysis reveals that the 28 kDa protein shares a modest degree of homology with a member of the E. coli heat shock protein family.
