Characterization, expression and envelope association of a Chlamydia trachomatis 28 kDa protein.
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.
Schmiel
D H
DH
Department of Microbiology and Immunology, University of North Carolina School of Medicine, Chapel Hill 27599, USA.
Raulston
J E
JE
Fox
E
E
Wyrick
P B
PB
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics*; D001483:Base Sequence; D002692:Chlamydia trachomatis / Q000737:chemistry* / Q000235:genetics / Q000254:growth & development; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D008969:Molecular Sequence Data
C104707:28-kDa protein, Chlamydia; D001425:Bacterial Outer Membrane Proteins; D004269:DNA, Bacterial