The RhopH complex is transferred to the host cell cytoplasm following red blood cell invasion by Plasmodium falciparum

Molecular and Biochemical Parasitology

Volumn 160, Issue 2, 2008, Pages 81-89

  Vincensini, Laetitia ^a   Fall, Gamou ^b   Berry, Laurence ^b   Blisnick, Thierry ^a   Braun Breton, Catherine ^a,b  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

Author keywords

Cytoadherence; Malaria parasite; Maurer's clefts; Protein export; Rhoptries

Indexed keywords

PROTEIN RHOPH; PROTOZOAL PROTEIN;

ARTICLE; CELL ADHESION; CELL INVASION; CONTROLLED STUDY; CYTOPLASM; ERYTHROCYTE; HOST CELL; IMMUNOPRECIPITATION; MEROZOITE; NONHUMAN; PHENOTYPE; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN TRANSPORT;

ANIMALS; BLOTTING, WESTERN; CYTOPLASM; ERYTHROCYTES; IMMUNOPRECIPITATION; MICROSCOPY, FLUORESCENCE; PLASMODIUM FALCIPARUM; PROTEIN TRANSPORT; PROTOZOAN PROTEINS;

PLASMODIUM FALCIPARUM;

EID: 50049118024     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2008.04.002     Document Type: Article

References (28)

1. Hinterberg K., Scherf A., Gysin J., et al. Plasmodium falciparum: the Pf332 antigen is secreted from the parasite by a brefeldin A-dependent pathway and is translocated to the erythrocyte membrane via the Maurer's clefts. Exp Parasitol 79 (1994) 279-291
2. Wickham M.E., Rug M., Ralph S.A., et al. Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes. EMBO J 20 (2001) 5636-5649
3. Haldar K., Mohandas N., Samuel B.U., et al. Protein and lipid trafficking induced in erythrocytes infected by malaria parasites. Cell Microbiol 4 (2002) 383-395
4. Adisa A., Albano F.R., Reeder J., Foley M., and Tilley L. Evidence for a role for a Plasmodium falciparum homologue of Sec31p in the export of proteins to the surface of malaria parasite-infected erythrocytes. J Cell Sci 114 (2001) 3377-3386
5. Hayashi M., Taniguchi S., Ishizuka Y., et al. A homologue of N-ethylmaleimide-sensitive factor in the malaria parasite Plasmodium falciparum is exported and localized in vesicular structures in the cytoplasm of infected erythrocytes in the brefeldin A-sensitive pathway. J Biol Chem 276 (2001) 15249-15255
6. Blisnick T., Vincensini L., Fall G., and Braun Breton C. PP1 phosphatase, a Plasmodium falciparum essential enzyme, is exported to the host cell and implicated in the release of infectious merozoites. Cell Microbiol 8 April (4) (2006) 591-601
7. Vincensini L., Richert S., Blisnick T., et al. Proteomic analysis identifies novel proteins of the Maurer's clefts, a secretory compartment delivering Plasmodium falciparum proteins to the surface of its host cell. Mol Cell Proteomics 4 (2005) 582-596
8. Blisnick T., Morales Betoulle M.E., Barale J.C., et al. Pfsbp1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton. Mol Biochem Parasitol 111 (2000) 107-121
9. Bannister L.H., Mitchell G.H., Butcher G.A., and Dennis E.D. Lamellar membranes associated with rhoptries in erythrocytic merozoites of Plasmodium knowlesi: a clue to the mechanism of invasion. Parasitology 92 (1986) 291-303
10. Cooper J.A., Ingram L.T., Bushell G.R., et al. The 140/130/105 kiloDalton protein complex in the rhoptries of Plasmodium falciparum consists of discrete polypeptides. Mol Biochem Parasitol 29 (1988) 251-260
11. Brown H.J., and Coppel R.L. Primary structure of a Plasmodium falciparum rhoptry antigen. Mol Biochem Parasitol 49 (1991) 99-110
12. Kaneko O., Tsuboi T., Ling I.T., et al. The high molecular mass rhoptry protein, RhopH1, is encoded by members of the clag multigene family in Plasmodium falciparum and Plasmodium yoelii. Mol Biochem Parasitol 118 (2001) 223-231
13. Ling I.T., Kaneko O., Narum D.L., et al. Characterisation of the rhoph2 gene of Plasmodium falciparum and Plasmodium yoelii. Mol Biochem Parasitol 127 (2003) 47-57
14. Sam-Yellowe T.Y., Shio H., and Perkins M.E. Secretion of Plasmodium falciparum rhoptry protein into the plasma membrane of host erythrocytes. J Cell Biol 106 (1988) 1507-1513
15. Sam-Yellowe T.Y., and Perkins M.E. Interaction of the 140/130/110 kDa rhoptry protein complex of Plasmodium falciparum with the erythrocyte membrane and liposomes. Exp Parasitol 73 (1991) 161-171
16. Hiller N.L., Akompong T., Morrow J.S., Holder A.A., and Haldar K. Identification of a stomatin orthologue in vacuoles induced in human erythrocytes by malaria parasites: a role for microbial raft-proteins in apicomplexan vacuole biogenesis. J Biol Chem 278 (2003) 48413-48421
17. Braun-Breton C., Jendoubi M., Brunet E., Perrin L., Scaife J., and Pereira da Silva L. In vivo time course of synthesis and processing of major schizont membrane polypeptides in Plasmodium falciparum. Mol Biochem Parasitol 20 (1986) 33-43
18. Pasvol G., Wilson R.J., Smalley M.E., and Brown J. Separation of viable schizont-infected red cells of Plasmodium falciparum from human blood. Ann Trop Med Parasitol 72 (1978) 87-88
19. Smith D.B., and Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67 (1988) 31-40
20. Frangioni J.V., and Neel B.G. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal Biochem 210 (1993) 179-187
21. Lustigman S., Anders R.F., Brown G.V., and Coppel R.L. A component of an antigenic rhoptry complex of Plasmodium falciparum is modified after merozoite invasion. Mol Biochem Parasitol 30 (1988) 217-224
22. Ling I.T., Florens L., Dluzewski A.R., et al. The Plasmodium falciparum clag9 gene encodes a rhoptry protein that is transferred to the host erythrocyte upon invasion. Mol Microbiol 52 (2004) 107-118
23. Ansorge I., Benting J., Bhakdi S., and Lingelbach K. Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O. Biochem J 315 (1996) 307-314
24. Sam-Yellowe T.Y., Fujioka H., Aikawa M., Hall T., and Drazba J.A. A Plasmodium falciparum protein located in Maurer's clefts underneath knobs and protein localization in association with Rhop-3 and SERA in the intracellular network of infected erythrocytes. Parasitol Res 87 (2001) 173-185
25. Leech J.H., Barnwell J.W., Aikawa M., Miller L.H., and Howard R.J. Plasmodium falciparum malaria: association of knobs on the surface of infected erythrocytes with a histidine-rich protein and the erythrocyte skeleton. J Cell Biol 98 (1984) 1256-1264
26. Papakrivos J., Newbold C.I., and Lingelbach K. A potential novel mechanism for the insertion of a membrane protein revealed by a biochemical analysis of the Plasmodium falciparum cytoadherence molecule PfEMP-1. Mol Microbiol 55 (2005) 1272-1284
27. Kriek N., Tilley L., Horrocks P., et al. Characterization of the pathway for transport of the cytoadherence-mediating protein, PfEMP1, to the host cell surface in malaria parasite-infected erythrocytes. Mol Microbiol 50 (2003) 1215-1227
28. Trenholme K.R., Gardiner D.L., Holt D.C., Thomas E.A., Cowman A.F., and Kemp D.J. Clag9: a cytoadherence gene in Plasmodium falciparum essential for binding of parasitized erythrocytes to CD36. Proc Natl Acad Sci USA 97 (2000) 4029-4033