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Originally published In Press as doi:10.1074/jbc.M209837200 on December 5, 2002

J. Biol. Chem., Vol. 278, Issue 8, 6229-6234, February 21, 2003
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C-terminal Processing of the Toxoplasma Protein MIC2 Is Essential for Invasion into Host Cells*

Fabien Brossier, Travis J. JewettDagger , Jennie L. LovettDagger , and L. David Sibley§

From the Department of Molecular Microbiology, Washington University School of Medicine, Saint Louis, Missouri 63110

Host cell invasion by apicomplexan parasites is accompanied by the rapid, polarized secretion of parasite proteins that are involved in cell attachment. The Toxoplasma gondii micronemal protein MIC2 contains several extracellular adhesive domains, a transmembrane domain, and a short cytoplasmic tail. Following apical secretion, MIC2 is transiently present on the parasite surface before being translocated backward and released by proteolytic cleavage. Mutations in the extracellular domain of MIC2, directly upstream of the transmembrane domain, prevented processing and release of the soluble protein into the supernatant. A conserved basic residue in MIC2 was essential for cleavage, and basic residues are similarly positioned in other microneme proteins. Following the induction of secretion, MIC2 processing mutants were stably expressed on the surface of the parasite. Surface MIC2-expressing mutants showed increased adhesion to host cells, yet were impaired in their capacity to invade. These data demonstrate that proteolysis is essential for releasing cell surface adhesins prior to cell entry by apicomplexan parasites.

* This work was supported in part by National Institutes of Health Grant AI34036.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Partially supported by National Institutes of Health Institutional Training Grant AI010172 (to Washington University).

§ Recipient of a Scholar Award in Molecular Parasitology from the Burroughs Wellcome Fund and to whom correspondence should be addressed. Tel.: 314-362-8873; Fax: 314-362-3203; E-mail: sibley@borcim.wustl.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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