Biosynthesis, localization, and macromolecular arrangement of the plasmodium falciparum translocon of exported proteins (PTEX)

Bullen, Hayley E., Charnaud, Sarah C., Kalanon, Ming, Riglar, David T., Dekiwadia, Chaitali, Kangwanrangsan, Niwat, Torii, Motomi, Tsuboi, Takafumi, Baum, Jacob, Ralph, Stuart A., Cowman, Alan F., de Koning-Ward, Tania F., Crabb, Brendan S. and Gilson, Paul R. 2012, Biosynthesis, localization, and macromolecular arrangement of the plasmodium falciparum translocon of exported proteins (PTEX), Journal of biological chemistry, vol. 287, no. 11, pp. 7871-7884.

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Title Biosynthesis, localization, and macromolecular arrangement of the plasmodium falciparum translocon of exported proteins (PTEX)
Formatted title Biosynthesis, localization, and macromolecular arrangement of the plasmodium falciparum translocon of exported proteins (PTEX)
Author(s) Bullen, Hayley E.
Charnaud, Sarah C.
Kalanon, Ming
Riglar, David T.
Dekiwadia, Chaitali
Kangwanrangsan, Niwat
Torii, Motomi
Tsuboi, Takafumi
Baum, Jacob
Ralph, Stuart A.
Cowman, Alan F.
de Koning-Ward, Tania F.
Crabb, Brendan S.
Gilson, Paul R.
Journal name Journal of biological chemistry
Volume number 287
Issue number 11
Start page 7871
End page 7884
Total pages 13
Publisher American Society for Biochemistry and Molecular Biology
Place of publication Bethesda, Md.
Publication date 2012-03
ISSN 0021-9258
Keyword(s) malaria parasites
dense granules
host erythrocyte
membrane
clya
virulence
reveals
vaccine
toxin
Summary To survive within its host erythrocyte, Plasmodium falciparum must export hundreds of proteins across both its parasite plasma membrane and surrounding parasitophorous vacuole membrane, most of which are likely to use a protein complex known as PTEX (Plasmodium translocon of exported proteins). PTEX is a putative protein trafficking machinery responsible for the export of hundreds of proteins across the parasitophorous vacuole membrane and into the human host cell. Five proteins are known to comprise the PTEX complex, and in this study, three of the major stoichiometric components are investigated including HSP101 (a AAA+ ATPase), a protein of no known function termed PTEX150, and the apparent membrane component EXP2. We show that these proteins are synthesized in the preceding schizont stage (PTEX150 and HSP101) or even earlier in the life cycle (EXP2), and before invasion these components reside within the dense granules of invasive merozoites. From these apical organelles, the protein complex is released into the host cell where it resides with little turnover in the parasitophorous vacuole membrane for most of the remainder of the following cell cycle. At this membrane, PTEX is arranged in a stable macromolecular complex of >1230 kDa that includes an ∼600-kDa apparently homo-oligomeric complex of EXP2 that can be separated from the remainder of the PTEX complex using non-ionic detergents. Two different biochemical methods undertaken here suggest that PTEX components associate as EXP2-PTEX150-HSP101, with EXP2 associating with the vacuolar membrane. Collectively, these data support the hypothesis that EXP2 oligomerizes and potentially forms the putative membrane-spanning pore to which the remainder of the PTEX complex is attached.
Language eng
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2012, American Society for Biochemistry and Molecular Biology
Persistent URL http://hdl.handle.net/10536/DRO/DU:30046623

Document type: Journal Article
Collection: School of Medicine
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Created: Tue, 07 Aug 2012, 21:38:27 EST by Tania de Koning-Ward

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