Protein Disulfide Isomerase, a Component of the Estrogen Receptor Complex, Is Associated withChlamydia trachomatisSerovar E Attached to Human Endometrial Epithelial Cells
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Medientyp:
E-Artikel
Titel:
Protein Disulfide Isomerase, a Component of the Estrogen Receptor Complex, Is Associated withChlamydia trachomatisSerovar E Attached to Human Endometrial Epithelial Cells
Beteiligte:
Davis, C. H.;
Raulston, J. E.;
Wyrick, P. B.
Erschienen:
American Society for Microbiology, 2002
Erschienen in:Infection and Immunity
Sprache:
Englisch
DOI:
10.1128/iai.70.7.3413-3418.2002
ISSN:
0019-9567;
1098-5522
Entstehung:
Anmerkungen:
Beschreibung:
<jats:title>ABSTRACT</jats:title><jats:p><jats:italic>Chlamydia trachomatis</jats:italic>serovar E, the leading bacterial agent responsible for sexually transmitted diseases, is required to invade genital epithelial cells for its growth and survival, yet little is known about the adhesin-receptor interactions promoting its entry. In contrast, much has been published on the heparan sulfate receptor for binding<jats:italic>C. trachomatis</jats:italic>L2 elementary bodies (EBs) prior to entry into HeLa cells. Using a different experimental approach in which a biotinylated apical membrane protein receptor(s) attached to EB at 4°C was stripped off the surface of polarized HEC-1B cells and immunoprecipitated with polyclonal anti-EB antibodies, an ∼55-kDa protein was reproducibly detected by enhanced chemiluminescence and two-dimensional gel electrophoresis. Matrix-assisted laser desorption ionization mass-spectrometry sequence analysis revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estrogen receptor complex which carries out thiol-disulfide exchange reactions at infected host cell surfaces. Exposure of HEC-1B cells during EB attachment (1.5 to 2 h) to three different inhibitors of PDI reductive reactions—(i) the thiol-alkylating reagent DTNB (5,5′-dithiobis[2-nitrobenzoic acid]), (ii) bacitracin, and (iii) anti-PDI antibodies—resulted in reduced chlamydial infectivity. Since (i)<jats:italic>C. trachomatis</jats:italic>serovar E attachment to estrogen-dominant primary human endometrial epithelial cells is dramatically enhanced and (ii) productive entry into and infectivity of EB in host cells is dependent on reduction of EB cross-linked outer membrane proteins at the host cell surface, these data provide some preliminary evidence for an intriguing new potential receptor candidate for further analysis of luminal<jats:italic>C. trachomatis</jats:italic>serovar E entry.</jats:p>