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Infection and Immunity, December 2007, p. 5586-5596, Vol. 75, No. 12
0019-9567/07/$08.00+0     doi:10.1128/IAI.01020-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Chlamydia pneumoniae Inclusion Membrane Protein Cpn0585 Interacts with Multiple Rab GTPases{triangledown}

Claudio Cortes,1 Kimberly A. Rzomp,2 Amy Tvinnereim,1 Marci A. Scidmore,2 and Benjamin Wizel1*

Department of Microbiology and Immunology, University of Texas Health Center, Tyler, Texas 75708,1 Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York 148532

Received 25 July 2007/ Returned for modification 21 August 2007/ Accepted 17 September 2007

Chlamydiae are intracellular bacteria that develop within a membrane-bound vacuole called an inclusion. To ensure that the inclusion is a safe niche for chlamydial replication, chlamydiae exploit a number of host cell processes, including membrane-trafficking pathways. Recently, several Rab GTPases were found to associate with the inclusions of various chlamydial species. Here we report that Cpn0585, a Chlamydia pneumoniae inclusion membrane protein (Inc), interacts with multiple Rab GTPases. The results from yeast two-hybrid experiments revealed that an amino-terminally truncated form of Cpn0585 (Cpn0585102-651) interacts with Rab1, Rab10, and Rab11 but not with Rab4 or Rab6. Cpn0585-Rab GTPase interactions are direct and GTP dependent as shown in glutathione S-transferase pull-down assays using native and recombinant Cpn0585. In C. pneumoniae-infected HEp-2 cells transfected with enhanced green fluorescent protein (EGFP)-tagged Rab GTPases, the colocalization with Cpn0585 at the inclusion membrane was partial for EGFP-Rab1 and EGFP-Rab10, but extensive for wild-type EGFP-Rab11A and the constitutively active GTPase-deficient EGFP-Rab11AQ70L. Moreover, Cpn0585 colocalized with EGFP-Rab11AQ70L as early as 2 h postinfection. Upon delivery into live C. pneumoniae-infected cells, Cpn0585628-651-specific antibodies bound to the inclusion membrane, demonstrating that the Rab GTPase-interacting domain of Cpn0585 faces the host cell cytosol. Finally, ectopic expression of Cpn0585102-651 partially inhibited the development of C. pneumoniae inclusions in EGFP. but not in EGFP-Rab11AQ70L-expressing HEp-2 cells. Collectively, these data suggest that Cpn0585 is involved in the recruitment of Rab GTPases to the inclusion membrane and that interfering with this function may adversely impact the fitness of the C. pneumoniae inclusion for chlamydial replication.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, University of Texas Health Center, Tyler, TX 75708. Phone: (903) 877-5872. Fax: (903) 877-7989. E-mail: bwizel{at}uthct.edu

{triangledown} Published ahead of print on 1 October 2007.

Editor: R. P. Morrison

Infection and Immunity, December 2007, p. 5586-5596, Vol. 75, No. 12
0019-9567/07/$08.00+0     doi:10.1128/IAI.01020-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hasegawa, A., Sogo, L. F., Tan, M., Sutterlin, C. (2009). Host Complement Regulatory Protein CD59 Is Transported to the Chlamydial Inclusion by a Golgi Apparatus-Independent Pathway. Infect. Immun. 77: 1285-1292 [Abstract] [Full Text]  


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