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Infection and Immunity, November 2008, p. 4842-4850, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00715-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Chlamydial Effector Proteins Localized to the Host Cell Cytoplasmic Compartment{triangledown}

Betsy Kleba{dagger} and Richard S. Stephens*

Program in Infectious Diseases and Immunity, University of California, Berkeley, California 94720

Received 6 June 2008/ Returned for modification 5 July 2008/ Accepted 6 August 2008

Disease-causing microbes utilize various strategies to modify their environment in order to create a favorable location for growth and survival. Gram-negative bacterial pathogens often use specialized secretion systems to translocate effector proteins directly into the cytosol of the eukaryotic cells they infect. These bacterial proteins are responsible for modulating eukaryotic cell functions. Identification of the bacterial effectors has been a critical step toward understanding the molecular basis for the pathogenesis of the bacteria that use them. Chlamydiae are obligate intracellular bacterial pathogens that have a type III secretion system believed to translocate virulence effector proteins into the cytosol of their host cells. Selective permeabilization of the eukaryotic cell membrane was used in conjunction with metabolic labeling of bacterial proteins to identify chlamydial proteins that localize within the cytosol of infected cells. More than 20 Chlamydia trachomatis and C. pneumoniae proteins were detected within the cytoplasmic compartment of infected cells. While a number of cytosolic proteins were shared, others were unique to each species, suggesting that variation among cytosolic chlamydial proteins contributes to the differences in the pathogenesis of the chlamydial species. The spectrum of chlamydial proteins exported differed concomitant with the progress of the developmental cycle. These data confirm that a dynamic relationship exists between Chlamydia and its host and that translocation of bacterial proteins into the cytosol is developmentally dependent.

* Corresponding author. Mailing address: Division of Infectious Diseases, School of Public Health, 16 Barker Hall, University of California, Berkeley, CA 94720. Phone: (510) 643-9900. Fax: (510) 643-1537. E-mail: RSS{at}Berkeley.edu

{triangledown} Published ahead of print on 18 August 2008.

Editor: A. J. Bäumler

{dagger} Present address: Host-Parasite Interactions Section, Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840.

Infection and Immunity, November 2008, p. 4842-4850, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00715-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Swanson, K. A., Taylor, L. D., Frank, S. D., Sturdevant, G. L., Fischer, E. R., Carlson, J. H., Whitmire, W. M., Caldwell, H. D. (2009). Chlamydia trachomatis Polymorphic Membrane Protein D Is an Oligomeric Autotransporter with a Higher-Order Structure. Infect. Immun. 77: 508-516 [Abstract] [Full Text]  


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