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Infection and Immunity, January 2009, p. 508-516, Vol. 77, No. 1
0019-9567/09/$08.00+0     doi:10.1128/IAI.01173-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Chlamydia trachomatis Polymorphic Membrane Protein D Is an Oligomeric Autotransporter with a Higher-Order Structure{triangledown}

Kena A. Swanson,1,{dagger} Lacey D. Taylor,1,{dagger} Shaun D. Frank,1 Gail L. Sturdevant,1 Elizabeth R. Fischer,2 John H. Carlson,1 William M. Whitmire,1 and Harlan D. Caldwell1*

Laboratory of Intracellular Parasites,1 Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 598402

Received 19 September 2008/ Returned for modification 22 October 2008/ Accepted 2 November 2008

Chlamydia trachomatis is a globally important obligate intracellular bacterial pathogen that is a leading cause of sexually transmitted disease and blinding trachoma. Effective control of these diseases will likely require a preventative vaccine. C. trachomatis polymorphic membrane protein D (PmpD) is an attractive vaccine candidate as it is conserved among C. trachomatis strains and is a target of broadly cross-reactive neutralizing antibodies. We show here that immunoaffinity-purified native PmpD exists as an oligomer with a distinct 23-nm flower-like structure. Two-dimensional blue native-sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses showed that the oligomers were composed of full-length PmpD (p155) and two proteolytically processed fragments, the p73 passenger domain (PD) and the p82 translocator domain. We also show that PmpD undergoes an infection-dependent proteolytic processing step late in the growth cycle that yields a soluble extended PD (p111) that was processed into a p73 PD and a novel p30 fragment. Interestingly, soluble PmpD peptides possess putative eukaryote-interacting functional motifs, implying potential secondary functions within or distal to infected cells. Collectively, our findings show that PmpD exists as two distinct forms, a surface-associated oligomer exhibiting a higher-order flower-like structure and a soluble form restricted to infected cells. We hypothesize that PmpD is a multifunctional virulence factor important in chlamydial pathogenesis and could represent novel vaccine or drug targets for the control of human chlamydial infections.

* Corresponding author. Mailing address: Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 903 South 4th St., Hamilton, MT 59840. Phone: (406) 363-9333. Fax: (406) 363-9380. E-mail: hcaldwell{at}niaid.nih.gov

{triangledown} Published ahead of print on 10 November 2008.

Editor: S. R. Blanke

{dagger} These authors contributed equally to this work.

Infection and Immunity, January 2009, p. 508-516, Vol. 77, No. 1
0019-9567/09/$08.00+0     doi:10.1128/IAI.01173-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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