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Infection and Immunity, July 2002, p. 3413-3418, Vol. 70, No. 7
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.7.3413-3418.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Protein Disulfide Isomerase, a Component of the Estrogen Receptor Complex, Is Associated with Chlamydia trachomatis Serovar E Attached to Human Endometrial Epithelial Cells

C. H. Davis,1 J. E. Raulston,1,2 and P. B. Wyrick1,2*

Department of Microbiology and Immunology, School of Medicine, University of North Carolina—Chapel Hill, Chapel Hill, North Carolina,1 Department of Microbiology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, Tennessee2

Received 9 January 2002/ Returned for modification 12 March 2002/ Accepted 27 March 2002

Chlamydia trachomatis 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 C. trachomatis 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) C. trachomatis 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 C. trachomatis serovar E entry.

* Corresponding author. Mailing address: Department of Microbiology, Box 70579, VA#1-Rm 1-41, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, TN 37614. Phone: (423) 439-8079. Fax: (423) 439-8044. E-mail: pbwyrick{at}etsu.edu.

Editor: D. L. Burns

Infection and Immunity, July 2002, p. 3413-3418, Vol. 70, No. 7
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.7.3413-3418.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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