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Differential targeting of dense granule proteins in the parasitophorous vacuole of Toxoplasma gondii

Published online by Cambridge University Press:  06 April 2009

A. Achbarou
Affiliation:
Unité 42 INSERM, 369 rue Jules Guesde, 59650 Villeneuve d'ascq, France
O. Mercereau-Puijalon
Affiliation:
Département de Parasitologie Expérimentale, Institut Pasteur, 28 rue du Dr. Roux, 75015 Paris, France
A. Sadak
Affiliation:
Unité 42 INSERM, 369 rue Jules Guesde, 59650 Villeneuve d'ascq, France
B. Fortier
Affiliation:
Unité 42 INSERM, 369 rue Jules Guesde, 59650 Villeneuve d'ascq, France
M. A. Leriche
Affiliation:
Unité 42 INSERM, 369 rue Jules Guesde, 59650 Villeneuve d'ascq, France
D. Camus
Affiliation:
Unité 42 INSERM, 369 rue Jules Guesde, 59650 Villeneuve d'ascq, France
J. F. Dubremetz
Affiliation:
Unité 42 INSERM, 369 rue Jules Guesde, 59650 Villeneuve d'ascq, France

Extract

The biosynthesis and fate of 4 different dense granule proteins of Toxoplasma gondii were studied with 3 monoclonal antibodies raised against tachyzoites and 1 polyclonal antibody raised against a recombinant protein. These proteins have the following molecular weights: 27 kDa (GRA 1), 28 kDa (GRA 2), 30 kDa (GRA 3) and 40 kDa (GRA 4). All four proteins were found in dense granules by immunoelectron microscopy; in T. gondii-infected cells, they were found in the vacuolar network but, in addition, GRA 3 was also detected on the parasitophorous vacuole membrane. Therefore, dense granule contents undergo differential targeting when exocytosed in the parasitophorous vacuole. Metabolic labelling and immunoprecipitation showed that GRA 2 and GRA 3 were processed from lower molecular weight precursors, and that GRA 2 and GRA 4 incorporated [3H] glucosamine and are thus likely to be glycosylated.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1991

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