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Infection and Immunity, May 2009, p. 1734-1745, Vol. 77, No. 5
0019-9567/09/$08.00+0     doi:10.1128/IAI.00027-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

An Ehrlichia chaffeensis Tandem Repeat Protein Interacts with Multiple Host Targets Involved in Cell Signaling, Transcriptional Regulation, and Vesicle Trafficking{triangledown}

Abdul Wakeel,1 Jeeba A. Kuriakose,1 and Jere W. McBride1,2,3,4*

Departments of Pathology,1 Microbiology and Immunology,2 Center for Biodefense and Emerging Infectious Diseases,3 Sealy Center for Vaccine Development, Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, Texas 77555-06094

Received 8 January 2009/ Returned for modification 14 February 2009/ Accepted 28 February 2009

Ehrlichia chaffeensis is an obligately intracellular bacterium that exhibits tropism for mononuclear phagocytes forming cytoplasmic membrane-bound microcolonies called morulae. To survive and replicate within phagocytes, E. chaffeensis exploits the host cell by modulating a number of host cell processes, but the ehrlichial effector proteins involved are unknown. In this study, we determined that p47, a secreted, differentially expressed, tandem repeat (TR) protein, interacts with multiple host proteins associated with cell signaling, transcriptional regulation, and vesicle trafficking. Yeast two-hybrid analysis revealed that p47 interacts with polycomb group ring finger 5 (PCGF5) protein, Src protein tyrosine kinase FYN (FYN), protein tyrosine phosphatase non-receptor type 2 (PTPN2), and adenylate cyclase-associated protein 1 (CAP1). p47 interaction with these proteins was further confirmed by coimmunoprecipitation assays and colocalization in HeLa cells transfected with p47-green fluorescent fusion protein (AcGFP1-p47). Moreover, confocal microscopy demonstrated p47-expressing dense-cored (DC) ehrlichiae colocalized with PCGF5, FYN, PTPN2, and CAP1. An amino-terminally truncated form of p47 containing TRs interacted only with PCGF5 and not with FYN, PTPN2, and CAP1, indicating differences in p47 domains that are involved in these interactions. These results demonstrate that p47 is involved in a complex network of interactions involving numerous host cell proteins. Furthermore, this study provides a new insight into the molecular and functional distinction of DC ehrlichiae, as well as the effector proteins involved in facilitating ehrlichial survival in mononuclear phagocytes.

* Corresponding author. Mailing address: Department of Pathology, Center for Biodefense and Emerging Infectious Diseases, University of Texas Medical Branch, Galveston, TX 77555-0609. Phone: (409) 747-2498. Fax: (409) 747-2455. E-mail: jemcbride{at}utmb.edu

{triangledown} Published ahead of print on 9 March 2009.

Editor: A. Camilli

Infection and Immunity, May 2009, p. 1734-1745, Vol. 77, No. 5
0019-9567/09/$08.00+0     doi:10.1128/IAI.00027-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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