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Volumn 511, Issue 7511, 2014, Pages 592-595

PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 101; HYBRID PROTEIN; PLASMODIUM TRANSLOCON OF EXPORTED PROTEIN; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 84905004491     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13574     Document Type: Article
Times cited : (212)

References (29)
  • 1
    • 84884505381 scopus 로고    scopus 로고
    • Plasmodium nesting: Remaking the erythrocyte from the inside out
    • Boddey, J. A. & Cowman, A. F. Plasmodium nesting: remaking the erythrocyte from the inside out. Annu. Rev. Microbiol. 67, 243-269 (2013).
    • (2013) Annu. Rev. Microbiol. , vol.67 , pp. 243-269
    • Boddey, J.A.1    Cowman, A.F.2
  • 2
    • 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 459, 945-949 (2009).
    • (2009) Nature , vol.459 , pp. 945-949
    • De Koning-Ward, T.F.1
  • 3
    • 84858011813 scopus 로고    scopus 로고
    • Biosyn thesis 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. 287, 7871-7884 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 7871-7884
    • Bullen, H.E.1
  • 4
    • 84879140486 scopus 로고    scopus 로고
    • Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes
    • Riglar, D. T. et al. Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes. NatureCommun. 4, 1415 (2013).
    • (2013) Nature Commun , vol.4 , pp. 1415
    • Riglar, D.T.1
  • 5
    • 77956972260 scopus 로고    scopus 로고
    • A general chemical method to regulate protein stability in the mammalian central nervous system
    • Iwamoto, M., Bjorklund, T., Lundberg, C., Kirik, D. & Wandless, T. J. A general chemical method to regulate protein stability in the mammalian central nervous system. Chem. Biol. 17, 981-988 (2010).
    • (2010) Chem. Biol. , vol.17 , pp. 981-988
    • Iwamoto, M.1    Bjorklund, T.2    Lundberg, C.3    Kirik, D.4    Wandless, T.J.5
  • 6
    • 79952732629 scopus 로고    scopus 로고
    • Asparagine repeat function in a Plasmodium falciparum protein assessed via a regulatable fluorescent affinity tag
    • Muralidharan, V., Oksman, A., Iwamoto, M., Wandless, T. J. & Goldberg, D. E. Asparagine repeat function in a Plasmodium falciparum protein assessed via a regulatable fluorescent affinity tag. Proc. Natl Acad. Sci. USA 108, 4411-4416 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 4411-4416
    • Muralidharan, V.1    Oksman, A.2    Iwamoto, M.3    Wandless, T.J.4    Goldberg, D.E.5
  • 7
    • 84871752624 scopus 로고    scopus 로고
    • Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers
    • Muralidharan, V., Oksman, A., Pal, P., Lindquist, S. & Goldberg, D. E. Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers. Nature Commun. 3, 1310 (2012).
    • (2012) Nature Commun. , vol.3 , pp. 1310
    • Muralidharan, V.1    Oksman, A.2    Pal, P.3    Lindquist, S.4    Goldberg, D.E.5
  • 8
    • 77954726224 scopus 로고    scopus 로고
    • Protein export marks the early phase of gametocytogenesis of the human malaria parasite Plasmodium falciparum
    • Silvestrini, F. et al. Protein export marks the early phase of gametocytogenesis of the human malaria parasite Plasmodium falciparum. Mol. Cell. Proteomics 9, 1437-1448 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1437-1448
    • Silvestrini, F.1
  • 9
    • 84884289227 scopus 로고    scopus 로고
    • The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growth
    • Matthews, K. et al. The Plasmodium translocon of exported proteins (PTEX) component thioredoxin-2 is important for maintaining normal blood-stage growth. Mol. Microbiol. 89, 1167-1186 (2013).
    • (2013) Mol. Microbiol. , vol.89 , pp. 1167-1186
    • Matthews, K.1
  • 10
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti, M., Good, R. T., Rug, M., Knuepfer, E. & Cowman, A. F. Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science 306, 1930-1933 (2004).
    • (2004) Science , vol.306 , pp. 1930-1933
    • Marti, M.1    Good, R.T.2    Rug, M.3    Knuepfer, E.4    Cowman, A.F.5
  • 11
    • 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 306, 1934-1937 (2004).
    • (2004) Science , vol.306 , pp. 1934-1937
    • Hiller, N.L.1
  • 12
    • 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 463, 632-636 (2010).
    • (2010) Nature , vol.463 , pp. 632-636
    • Russo, I.1
  • 13
    • 76249091034 scopus 로고    scopus 로고
    • An aspartyl protease directsmalaria effector proteins to the host cell
    • Boddey, J. A. et al. An aspartyl protease directsmalaria effector proteins to the host cell. Nature 463, 627-631 (2010).
    • (2010) Nature , vol.463 , pp. 627-631
    • Boddey, J.A.1
  • 14
    • 0023616658 scopus 로고
    • Comparative analysis of the Plasmodium falciparum histidine-rich proteins HRP-I, HRP-II and HRP-III in malaria parasites of diverse origin
    • Rock, E. P. et al. Comparative analysis of the Plasmodium falciparum histidine-rich proteins HRP-I, HRP-II and HRP-III in malaria parasites of diverse origin. Parasitology 95, 209-227 (1987).
    • (1987) Parasitology , vol.95 , pp. 209-227
    • Rock, E.P.1
  • 15
    • 33746640413 scopus 로고    scopus 로고
    • A cluster of ring stage-specific genes linked to a locus implicated in cytoadherence in Plasmodium falciparum codes for PEXEL-negative and PEXEL-positive proteins exported into the host cell
    • Spielmann, T. et al. A cluster of ring stage-specific genes linked to a locus implicated in cytoadherence in Plasmodium falciparum codes for PEXEL-negative and PEXEL-positive proteins exported into the host cell. Mol. Biol. Cell 17, 3613-3624 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3613-3624
    • Spielmann, T.1
  • 16
    • 0030904788 scopus 로고    scopus 로고
    • Targeted gene disruption shows that knobs enable malariainfected red cells to cytoadhereunderphysiologicalshear stress
    • Crabb, B. S. et al. Targeted gene disruption shows that knobs enable malariainfected red cells to cytoadhereunderphysiologicalshear stress.Cell89, 287-296 (1997).
    • (1997) Cell , vol.89 , pp. 287-296
    • Crabb, B.S.1
  • 17
    • 0025977921 scopus 로고
    • Plasmodium falciparum ring-infected erythrocyte surface antigen is released from merozoite dense granules after erythrocyte invasion
    • Culvenor, J. G., Day, K. P. & Anders, R. F. Plasmodium falciparum ring-infected erythrocyte surface antigen is released from merozoite dense granules after erythrocyte invasion. Infect. Immun. 59, 1183-1187 (1991).
    • (1991) Infect. Immun. , vol.59 , pp. 1183-1187
    • Culvenor, J.G.1    Day, K.P.2    Anders, R.F.3
  • 18
    • 84876115387 scopus 로고    scopus 로고
    • Role of plasmepsin v in export of diverse protein families from the Plasmodium falciparum exportome
    • Boddey, J. A. et al. Role of plasmepsin V in export of diverse protein families from the Plasmodium falciparum exportome. Traffic 14, 532-550 (2013).
    • (2013) Traffic , vol.14 , pp. 532-550
    • Boddey, J.A.1
  • 19
    • 84869168026 scopus 로고    scopus 로고
    • Uncovering common principles in protein export of malaria parasites
    • Grüring, C. et al. Uncovering common principles in protein export of malaria parasites. Cell Host Microbe 12, 717-729 (2012).
    • (2012) Cell Host Microbe , vol.12 , pp. 717-729
    • Grüring, C.1
  • 20
    • 84890279693 scopus 로고    scopus 로고
    • Maurer's clefts, the enigma of Plasmodium falciparum
    • Mundwiler-Pachlatko, E. & Beck, H. P. Maurer's clefts, the enigma of Plasmodium falciparum. Proc. Natl Acad. Sci. USA 110, 19987-19994 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 19987-19994
    • Mundwiler-Pachlatko, E.1    Beck, H.P.2
  • 21
    • 0033758215 scopus 로고    scopus 로고
    • Pfsbp1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton
    • Blisnick, T. et al.Pfsbp1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton. Mol. Biochem. Parasitol. 111, 107-121 (2000).
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 107-121
    • Blisnick, T.1
  • 22
    • 84883361050 scopus 로고    scopus 로고
    • Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export
    • Heiber, A. et al. Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export. PLoS Pathog. 9, e1003546 (2013).
    • (2013) PLoS Pathog , vol.9
    • Heiber, A.1
  • 24
    • 77956393490 scopus 로고    scopus 로고
    • Parasite-encoded Hsp40 proteins define novelmobile structures in the cytosol of the P falciparum-infected erythrocyte
    • Külzer, S. et al. Parasite-encoded Hsp40 proteins define novelmobile structures in the cytosol of the P. falciparum-infected erythrocyte. Cell. Microbiol. 12, 1398-1420 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 1398-1420
    • Külzer, S.1
  • 25
    • 0347122968 scopus 로고    scopus 로고
    • Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
    • Klemba, M., Beatty, W., Gluzman, I. & Goldberg, D. E. Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum. J. Cell Biol. 164, 47-56 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 47-56
    • Klemba, M.1    Beatty, W.2    Gluzman, I.3    Goldberg, D.E.4
  • 26
    • 36849090615 scopus 로고    scopus 로고
    • Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes
    • Yeoh, S. et al. Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes. Cell 131, 1072-1083 (2007).
    • (2007) Cell , vol.131 , pp. 1072-1083
    • Yeoh, S.1
  • 27
    • 80055108114 scopus 로고    scopus 로고
    • Functional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytes
    • Morahan, B. J. et al. Functional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytes. Eukaryot. Cell 10, 1492-1503 (2011).
    • (2011) Eukaryot. Cell , vol.10 , pp. 1492-1503
    • Morahan, B.J.1
  • 28
    • 79957553908 scopus 로고    scopus 로고
    • Malaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells
    • Nguitragool, W. et al. Malaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells. Cell 145, 665-677 (2011).
    • (2011) Cell , vol.145 , pp. 665-677
    • Nguitragool, W.1
  • 29
    • 60349121591 scopus 로고    scopus 로고
    • Export of a Toxoplasma gondii rhoptry neck protein complex at the host cell membrane to form the moving junction during invasion
    • Besteiro, S., Michelin, A., Poncet, J., Dubremetz, J. F. & Lebrun, M. Export of a Toxoplasma gondii rhoptry neck protein complex at the host cell membrane to form the moving junction during invasion. PLoS Pathog. 5, e1000309 (2009).
    • (2009) PLoS Pathog , vol.5
    • Besteiro, S.1    Michelin, A.2    Poncet, J.3    Dubremetz, J.F.4    Lebrun, M.5


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