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Volumn 28, Issue 12, 2012, Pages 555-562

Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites

Author keywords

Blood cells; Endoplasmic reticulum; Export; Host targeting; Malaria; Pathogenic secretion; Phosphoinositides

Indexed keywords

ASPARTIC PROTEINASE; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PLASMEPSIN V; UNCLASSIFIED DRUG;

EID: 84869183087     PISSN: 14714922     EISSN: 14715007     Source Type: Journal    
DOI: 10.1016/j.pt.2012.09.004     Document Type: Review
Times cited : (16)

References (33)
  • 1
    • 72849128957 scopus 로고    scopus 로고
    • Artemisinin combination therapy for malaria: beyond good efficacy
    • Price R.N., Douglas N.M. Artemisinin combination therapy for malaria: beyond good efficacy. Clin. Infect. Dis. 2009, 49:1638-1640.
    • (2009) Clin. Infect. Dis. , vol.49 , pp. 1638-1640
    • Price, R.N.1    Douglas, N.M.2
  • 2
    • 83455231470 scopus 로고    scopus 로고
    • Plasmodium knowlesi: a malaria parasite of monkeys and humans
    • Collins W.E. Plasmodium knowlesi: a malaria parasite of monkeys and humans. Annu. Rev. Entomol. 2012, 57:107-121.
    • (2012) Annu. Rev. Entomol. , vol.57 , pp. 107-121
    • Collins, W.E.1
  • 3
    • 0037034017 scopus 로고    scopus 로고
    • The pathogenic basis of malaria
    • Miller L.H., et al. The pathogenic basis of malaria. Nature 2002, 415:673-679.
    • (2002) Nature , vol.415 , pp. 673-679
    • Miller, L.H.1
  • 4
    • 84856104303 scopus 로고    scopus 로고
    • Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell
    • Bhattacharjee S., et al. Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell. Cell 2012, 148:201-212.
    • (2012) Cell , vol.148 , pp. 201-212
    • Bhattacharjee, S.1
  • 5
    • 34247115129 scopus 로고    scopus 로고
    • Erythrocyte remodeling by malaria parasites
    • Haldar K., Mohandas N. Erythrocyte remodeling by malaria parasites. Curr. Opin. Hematol. 2007, 14:203-209.
    • (2007) Curr. Opin. Hematol. , vol.14 , pp. 203-209
    • Haldar, K.1    Mohandas, N.2
  • 6
    • 80051559807 scopus 로고    scopus 로고
    • Genetic ablation of a Maurer's cleft protein prevents assembly of the Plasmodium falciparum virulence complex
    • Dixon M.W., et al. Genetic ablation of a Maurer's cleft protein prevents assembly of the Plasmodium falciparum virulence complex. Mol. Microbiol. 2011, 81:982-993.
    • (2011) Mol. Microbiol. , vol.81 , pp. 982-993
    • Dixon, M.W.1
  • 7
    • 0030953287 scopus 로고    scopus 로고
    • A membrane network for nutrient import in red cells infected with the malaria parasite
    • Lauer S.A., et al. A membrane network for nutrient import in red cells infected with the malaria parasite. Science 1997, 276:1122-1125.
    • (1997) Science , vol.276 , pp. 1122-1125
    • Lauer, S.A.1
  • 8
    • 33646926281 scopus 로고    scopus 로고
    • Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites
    • Sargeant T.J., et al. Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites. Genome Biol. 2006, 7:R12.
    • (2006) Genome Biol. , vol.7
    • Sargeant, T.J.1
  • 9
    • 46449088780 scopus 로고    scopus 로고
    • The malaria secretome: from algorithms to essential function in blood stage infection
    • van Ooij C., et al. The malaria secretome: from algorithms to essential function in blood stage infection. PLoS Pathog. 2008, 4:e1000084.
    • (2008) PLoS Pathog. , vol.4
    • van Ooij, C.1
  • 10
    • 10344245559 scopus 로고    scopus 로고
    • A host-targeting signal in virulence proteins reveals a secretome in malarial infection
    • Hiller N.L., et al. A host-targeting signal in virulence proteins reveals a secretome in malarial infection. Science 2004, 306:1934-1937.
    • (2004) Science , vol.306 , pp. 1934-1937
    • Hiller, N.L.1
  • 11
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti M., et al. Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science 2004, 306:1930-1933.
    • (2004) Science , vol.306 , pp. 1930-1933
    • Marti, M.1
  • 12
    • 50849084822 scopus 로고    scopus 로고
    • An erythrocyte vesicle protein exported by the malaria parasite promotes tubovesicular lipid import from the host cell surface
    • Tamez P.A., et al. An erythrocyte vesicle protein exported by the malaria parasite promotes tubovesicular lipid import from the host cell surface. PLoS Pathog. 2008, 4:e1000118.
    • (2008) PLoS Pathog. , vol.4
    • Tamez, P.A.1
  • 13
    • 17144386621 scopus 로고    scopus 로고
    • Protein transport and trafficking in Plasmodium falciparum-infected erythrocytes
    • Przyborski J.M., Lanzer M. Protein transport and trafficking in Plasmodium falciparum-infected erythrocytes. Parasitology 2005, 130:373-388.
    • (2005) Parasitology , vol.130 , pp. 373-388
    • Przyborski, J.M.1    Lanzer, M.2
  • 14
    • 33644895382 scopus 로고    scopus 로고
    • A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells
    • Cooke B.M., et al. A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells. J. Cell Biol. 2006, 172:899-908.
    • (2006) J. Cell Biol. , vol.172 , pp. 899-908
    • Cooke, B.M.1
  • 15
    • 72149083014 scopus 로고    scopus 로고
    • Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?
    • Spielmann T., Gilberger T.W. Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?. Trends Parasitol. 2010, 26:6-10.
    • (2010) Trends Parasitol. , vol.26 , pp. 6-10
    • Spielmann, T.1    Gilberger, T.W.2
  • 16
    • 58449127326 scopus 로고    scopus 로고
    • Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum
    • Gehde N., et al. Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum. Mol. Microbiol. 2009, 71:613-628.
    • (2009) Mol. Microbiol. , vol.71 , pp. 613-628
    • Gehde, N.1
  • 17
    • 48749112676 scopus 로고    scopus 로고
    • N-terminal processing of proteins exported by malaria parasites
    • Chang H.H., et al. N-terminal processing of proteins exported by malaria parasites. Mol. Biochem. Parasitol. 2008, 160:107-115.
    • (2008) Mol. Biochem. Parasitol. , vol.160 , pp. 107-115
    • Chang, H.H.1
  • 18
    • 59849124093 scopus 로고    scopus 로고
    • Role of the Plasmodium export element in trafficking parasite proteins to the infected erythrocyte
    • Boddey J.A., et al. Role of the Plasmodium export element in trafficking parasite proteins to the infected erythrocyte. Traffic 2009, 10:285-299.
    • (2009) Traffic , vol.10 , pp. 285-299
    • Boddey, J.A.1
  • 19
    • 77649340470 scopus 로고    scopus 로고
    • The host targeting motif in exported Plasmodium proteins is cleaved in the parasite endoplasmic reticulum
    • Osborne A.R., et al. The host targeting motif in exported Plasmodium proteins is cleaved in the parasite endoplasmic reticulum. Mol. Biochem. Parasitol. 2010, 171:25-31.
    • (2010) Mol. Biochem. Parasitol. , vol.171 , pp. 25-31
    • Osborne, A.R.1
  • 20
    • 76249091034 scopus 로고    scopus 로고
    • An aspartyl protease directs malaria effector proteins to the host cell
    • Boddey J.A., et al. An aspartyl protease directs malaria effector proteins to the host cell. Nature 2010, 463:627-631.
    • (2010) Nature , vol.463 , pp. 627-631
    • Boddey, J.A.1
  • 21
    • 76249123168 scopus 로고    scopus 로고
    • Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte
    • Russo I., et al. Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte. Nature 2010, 463:632-636.
    • (2010) Nature , vol.463 , pp. 632-636
    • Russo, I.1
  • 22
    • 24944499610 scopus 로고    scopus 로고
    • Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch
    • Lee S.A., et al. Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:13052-13057.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13052-13057
    • Lee, S.A.1
  • 23
    • 84862182124 scopus 로고    scopus 로고
    • Phosphoinositides and vesicular membrane traffic
    • Mayinger P. Phosphoinositides and vesicular membrane traffic. Biochim. Biophys. Acta 2012, 1821:1104-1113.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1104-1113
    • Mayinger, P.1
  • 24
    • 77954649564 scopus 로고    scopus 로고
    • Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of Early Endosomal Autoantigen 1 (EEA1)
    • Mishra A., et al. Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of Early Endosomal Autoantigen 1 (EEA1). Proc. Natl. Acad. Sci. U.S.A. 2010, 107:10866-10871.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10866-10871
    • Mishra, A.1
  • 25
    • 77957780616 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate, an essential lipid in Plasmodium, localizes to the food vacuole membrane and the apicoplast
    • Tawk L., et al. Phosphatidylinositol 3-phosphate, an essential lipid in Plasmodium, localizes to the food vacuole membrane and the apicoplast. Eukaryot. Cell 2010, 9:1519-1530.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1519-1530
    • Tawk, L.1
  • 26
    • 9444266430 scopus 로고    scopus 로고
    • The apicoplast: a review of the derived plastid of apicomplexan parasites
    • Waller R.F., McFadden G.I. The apicoplast: a review of the derived plastid of apicomplexan parasites. Curr. Issues Mol. Biol. 2005, 7:57-79.
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 57-79
    • Waller, R.F.1    McFadden, G.I.2
  • 27
    • 79952239104 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-monophosphate is involved in toxoplasma apicoplast biogenesis
    • Tawk L., et al. Phosphatidylinositol 3-monophosphate is involved in toxoplasma apicoplast biogenesis. PLoS Pathog. 2010, 7:e1001286.
    • (2010) PLoS Pathog. , vol.7
    • Tawk, L.1
  • 28
    • 77950612934 scopus 로고    scopus 로고
    • PfPI3K, a phosphatidylinositol-3 kinase from Plasmodium falciparum, is exported to the host erythrocyte and is involved in hemoglobin trafficking
    • Vaid A., et al. PfPI3K, a phosphatidylinositol-3 kinase from Plasmodium falciparum, is exported to the host erythrocyte and is involved in hemoglobin trafficking. Blood 2010, 115:2500-2507.
    • (2010) Blood , vol.115 , pp. 2500-2507
    • Vaid, A.1
  • 29
    • 77955041178 scopus 로고    scopus 로고
    • External lipid PI3P mediates entry of eukaryotic pathogen effectors into plant and animal host cells
    • Kale S.D., et al. External lipid PI3P mediates entry of eukaryotic pathogen effectors into plant and animal host cells. Cell 2010, 142:284-295.
    • (2010) Cell , vol.142 , pp. 284-295
    • Kale, S.D.1
  • 30
    • 33646906197 scopus 로고    scopus 로고
    • The malarial host-targeting signal is conserved in the Irish potato famine pathogen
    • Bhattacharjee S., et al. The malarial host-targeting signal is conserved in the Irish potato famine pathogen. PLoS Pathog. 2006, 2:e50.
    • (2006) PLoS Pathog. , vol.2
    • Bhattacharjee, S.1
  • 31
    • 0142059795 scopus 로고    scopus 로고
    • Cooperative domains define a unique host cell-targeting signal in Plasmodium falciparum-infected erythrocytes
    • Lopez-Estrano C., et al. Cooperative domains define a unique host cell-targeting signal in Plasmodium falciparum-infected erythrocytes. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:12402-12407.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12402-12407
    • Lopez-Estrano, C.1
  • 32
    • 67649277651 scopus 로고    scopus 로고
    • A newly discovered protein export machine in malaria parasites
    • de Koning-Ward T.F., et al. A newly discovered protein export machine in malaria parasites. Nature 2009, 459:945-949.
    • (2009) Nature , vol.459 , pp. 945-949
    • de Koning-Ward, T.F.1
  • 33
    • 84858011813 scopus 로고    scopus 로고
    • Biosynthesis, localization, and macromolecular arrangement of the Plasmodium falciparum translocon of exported proteins (PTEX)
    • Bullen H.E., et al. Biosynthesis, localization, and macromolecular arrangement of the Plasmodium falciparum translocon of exported proteins (PTEX). J. Biol. Chem. 2012, 287:7871-7884.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7871-7884
    • Bullen, H.E.1


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