Eukaryotic Cell Visit the journal of Applied and Environmental Biology
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EC Accepts, published online ahead of print on 4 April 2008
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Eukaryotic Cell doi:10.1128/EC.00413-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Molecular signals in the trafficking of the Toxoplasma gondii protein MIC3 to the micronemes

Hiba El Hajj, Julien Papoin, Odile Cérède, Nathalie Garcia-Réguet, Martine Soête, Jean-François Dubremetz, and Maryse Lebrun*

UMR 5235 CNRS, Université de Montpellier 2, CP 107, Place Eugène Bataillon, 34090 Montpellier, France; FRE 2377 CNRS, Institut de Biologie de Lille, 1 rue du professeur Calmette, 59021 Lille, France; UMR Université-INRA d'Immunologie Parasitaires, Faculté des Sciences Pharmaceutiques et Biologiques, 31 Avenue Monge, 37200 Tours, France

* To whom correspondence should be addressed. Email: maryse.lebrun{at}univ-montp2.fr.


   Abstract

The protozoan parasite Toxoplasma gondii is equipped with a sophisticated secretory apparatus including three distinct exocytic organelles named micronemes, rhoptries and dense granules. We have dissected the requirements for targeting the microneme protein MIC3, a key component of T. gondii infection. We have shown that MIC3 is processed in a post-Golgi compartment, and that the MIC3 pro-peptide and epidermal growth factor (EGF) modules contain microneme targeting information. The minimal requirement for microneme delivery is defined by the pro-peptide plus any one of the three EGF domains. We have demonstrated that the cleavage of the pro-peptide, the dimerization of MIC3 and the chitin-binding-like sequence, which are crucial for host cell binding and virulence, are dispensable for proper targeting. Finally, we have shown that part of MIC3 is withheld in the secretory pathway in a cell cycle-dependant manner.







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