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Published 9 July 2001. doi:10.1083/jcb.200101073
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© The Rockefeller University Press, 0021-9525/2001/7/95 $5.00
The Journal of Cell Biology, Volume 154, Number 1, July 9, 2001 95-108

Article

 The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane

Anthony P. Sinai1,2 and Keith A. Joiner1

1 Infectious Diseases Section, Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06520
2 Department of Microbiology and Immunology, University of Kentucky College of Medicine, Lexington, KY 40536

Address correspondence to Dr. Keith Joiner, LCI 808, Infectious Diseases Section, Department of Internal Medicine, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06520. Tel.: (203) 785-4140. Fax: (203) 785-3864. E-mail: keith.joiner{at}yale.edu; sinai{at}pop.uky.edu

Toxoplasma gondii replicates within a specialized vacuole surrounded by the parasitophorous vacuole membrane (PVM). The PVM forms intimate interactions with host mitochondria and endoplasmic reticulum (ER) in a process termed PVM–organelle association. In this study we identify a likely mediator of this process, the parasite protein ROP2. ROP2, which is localized to the PVM, is secreted from anterior organelles termed rhoptries during parasite invasion into host cells. The NH2-terminal domain of ROP2 (ROP2hc) within the PVM is exposed to the host cell cytosol, and has characteristics of a mitochondrial targeting signal. In in vitro assays, ROP2hc is partially translocated into the mitochondrial outer membrane and behaves like an integral membrane protein. Although ROP2hc does not translocate across the ER membrane, it does exhibit carbonate-resistant binding to this organelle. In vivo, ROP2hc expressed as a soluble fragment in the cytosol of uninfected cells associates with both mitochondria and ER. The 30–amino acid (aa) NH2-terminal sequence of ROP2hc, when fused to green fluorescent protein (GFP), is sufficient for mitochondrial targeting. Deletion of the 30-aa NH2-terminal signal from ROP2hc results in robust localization of the truncated protein to the ER. These results demonstrate a new mechanism for tight association of different membrane-bound organelles within the cell cytoplasm.

Key Words: Toxoplasma; ROP2; parasitophorous vacuole membrane; mitochondria; endoplasmic reticulum


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