메뉴 건너뛰기




Volumn 14, Issue 3, 2007, Pages 203-209

Erythrocyte remodeling by malaria parasites

Author keywords

Infection; Plasmodium falciparum; Red blood cells

Indexed keywords

ANTIGEN; CHAPERONE; MATURE ERYTHROCYTE SURFACE ANTIGEN; PROTOZOAL PROTEIN; RING INFECTED ERYTHROCYTE SURFACE ANTIGEN; UNCLASSIFIED DRUG;

EID: 34247115129     PISSN: 10656251     EISSN: 15317048     Source Type: Journal    
DOI: 10.1097/MOH.0b013e3280f31b2d     Document Type: Review
Times cited : (80)

References (44)
  • 2
    • 0027272883 scopus 로고
    • Red blood cell deformability, membrane material properties and shape: Regulation by transmembrane, skeletal and cytosolic proteins and lipids
    • Mohandas N, Chasis JA. Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids. Semin Hematol 1993; 30:171-192.
    • (1993) Semin Hematol , vol.30 , pp. 171-192
    • Mohandas, N.1    Chasis, J.A.2
  • 4
    • 0034307484 scopus 로고    scopus 로고
    • A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages
    • Bannister LH, Hopkins JM, Fowler RE, et al. A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages. Parasitol Today 2000; 16:427-433.
    • (2000) Parasitol Today , vol.16 , pp. 427-433
    • Bannister, L.H.1    Hopkins, J.M.2    Fowler, R.E.3
  • 5
    • 32944458099 scopus 로고    scopus 로고
    • Invasion of red blood cells by malaria parasites
    • Cowman AF, Crabb BS. Invasion of red blood cells by malaria parasites. Cell 2006; 124:755-766.
    • (2006) Cell , vol.124 , pp. 755-766
    • Cowman, A.F.1    Crabb, B.S.2
  • 6
    • 0027368604 scopus 로고
    • The origin of the parasitophorous vacuolar membrane lipids in malaria-infected red cells
    • Ward GE, Miller LH, Dvorak JA. The origin of the parasitophorous vacuolar membrane lipids in malaria-infected red cells. J Cell Sci 1993; 106:237-238.
    • (1993) J Cell Sci , vol.106 , pp. 237-238
    • Ward, G.E.1    Miller, L.H.2    Dvorak, J.A.3
  • 7
    • 0034679814 scopus 로고    scopus 로고
    • Vacuolar uptake of host components, and a role for cholesterol and sphingomyelin in malarial infection
    • Lauer SA, VanWye J, Harrison T, et al. Vacuolar uptake of host components, and a role for cholesterol and sphingomyelin in malarial infection. EMBO J 2000; 19:3556-3564.
    • (2000) EMBO J , vol.19 , pp. 3556-3564
    • Lauer, S.A.1    VanWye, J.2    Harrison, T.3
  • 8
    • 0035800734 scopus 로고    scopus 로고
    • The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection
    • Samuel BU, Mohandas N, Harrison T, et al. The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection. J Biol Chem 2001; 276:29319-29329.
    • (2001) J Biol Chem , vol.276 , pp. 29319-29329
    • Samuel, B.U.1    Mohandas, N.2    Harrison, T.3
  • 9
    • 0141654989 scopus 로고    scopus 로고
    • Erythrocyte G protein coupled receptor signaling in malaria infection
    • Harrison T, Samuel BU, Akompong T, et al. Erythrocyte G protein coupled receptor signaling in malaria infection. Science 2003; 301:1734-1736.
    • (2003) Science , vol.301 , pp. 1734-1736
    • Harrison, T.1    Samuel, B.U.2    Akompong, T.3
  • 10
    • 10744227416 scopus 로고    scopus 로고
    • Erythrocyte detergent-resistant membrane proteins: Their characterization and selective uptake during malarial infection
    • Murphy SC, Samuel BU, Harrison T, et al. Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection. Blood 2004; 103:1920-1928.
    • (2004) Blood , vol.103 , pp. 1920-1928
    • Murphy, S.C.1    Samuel, B.U.2    Harrison, T.3
  • 11
    • 0036771552 scopus 로고    scopus 로고
    • Detergent-resistant erythrocyte membrane rafts are modified by a Plasmodium falciparum infection
    • Nagao E, Seydel KB, Dvorak JA. Detergent-resistant erythrocyte membrane rafts are modified by a Plasmodium falciparum infection. Exp Parasitol 2002; 102:57-59.
    • (2002) Exp Parasitol , vol.102 , pp. 57-59
    • Nagao, E.1    Seydel, K.B.2    Dvorak, J.A.3
  • 12
    • 33645290220 scopus 로고    scopus 로고
    • Lipid rafts and malarial parasite infection of erythrocytes
    • Murphy S, Hiller NL, Harrison T, et al. Lipid rafts and malarial parasite infection of erythrocytes. Mol Membrane Biol 2006; 23:81-88.
    • (2006) Mol Membrane Biol , vol.23 , pp. 81-88
    • Murphy, S.1    Hiller, N.L.2    Harrison, T.3
  • 13
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linded proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP. Signal transducing molecules and glycosyl-phosphatidylinositol-linded proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 1993; 122:789-807.
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 14
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S, Brown DA, Linder ME. Lipid-dependent targeting of G proteins into rafts. J Biol Chem 2000; 275:2191-2198.
    • (2000) J Biol Chem , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 15
    • 33845875171 scopus 로고    scopus 로고
    • Erythrocyte G protein as a novel target for malarial chemotherapy
    • This study developed resealed erythrocyte ghosts capable of signaling and malaria infection as well as normal erythrocytes and used it to directly target erythrocyte Gs during invasion and growth of malaria parasites
    • Murphy SC, Harrison T, Hamm HE, et al. Erythrocyte G protein as a novel target for malarial chemotherapy. PLoS Med 2006; 3:e528. This study developed resealed erythrocyte ghosts capable of signaling and malaria infection as well as normal erythrocytes and used it to directly target erythrocyte Gs during invasion and growth of malaria parasites.
    • (2006) PLoS Med , vol.3
    • Murphy, S.C.1    Harrison, T.2    Hamm, H.E.3
  • 16
    • 0037606006 scopus 로고    scopus 로고
    • Novel epinephrine and cAMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion
    • Hines PC, Zen Q, Burney SN, et al. Novel epinephrine and cAMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion. Blood 2003; 101:3281-3287.
    • (2003) Blood , vol.101 , pp. 3281-3287
    • Hines, P.C.1    Zen, Q.2    Burney, S.N.3
  • 17
    • 0348111350 scopus 로고    scopus 로고
    • Identification of a stomatin orthologue in vacuoles induced in human erythrocytes by malaria parasites: A role for microbial raft proteins in apicomplexan vacuole biogenesis
    • Hiller NL, Akompong T, Morrow JS, et al. 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 2003; 278:48413-48421.
    • (2003) J Biol Chem , vol.278 , pp. 48413-48421
    • Hiller, N.L.1    Akompong, T.2    Morrow, J.S.3
  • 18
    • 0031408172 scopus 로고    scopus 로고
    • Regulation of red blood cell filterability by Ca+2 influx and cAMP-mediated signaling pathways
    • Oonishi T, Sakashita K, Uyesaka N. Regulation of red blood cell filterability by Ca+2 influx and cAMP-mediated signaling pathways. Am J Physiol 1997; 273:C1828-C1834.
    • (1997) Am J Physiol , vol.273
    • Oonishi, T.1    Sakashita, K.2    Uyesaka, N.3
  • 19
    • 0032578034 scopus 로고    scopus 로고
    • Mechanical fluctuations of the membrane-skeleton are dependent on F-actin ATPase in human erythrocytes
    • Tuvia S, Levin S, Bitler A, Korenstein R. Mechanical fluctuations of the membrane-skeleton are dependent on F-actin ATPase in human erythrocytes. J Cell Biol 1998; 141:1551-1561.
    • (1998) J Cell Biol , vol.141 , pp. 1551-1561
    • Tuvia, S.1    Levin, S.2    Bitler, A.3    Korenstein, R.4
  • 20
    • 0033134810 scopus 로고    scopus 로고
    • Beta-adrenergic agonists regulate cell membrane fluctuations of human erythrocytes
    • Tuvia S, Moses A, Gulayev N, et al. Beta-adrenergic agonists regulate cell membrane fluctuations of human erythrocytes. J Physiol 1999; 516 (Pt 3):781-792.
    • (1999) J Physiol , vol.516 , Issue.PART 3 , pp. 781-792
    • Tuvia, S.1    Moses, A.2    Gulayev, N.3
  • 21
    • 10344245559 scopus 로고    scopus 로고
    • A host-targeting signal in virulence proteins reveals a secretome in malarial infection
    • Hiller NL, Bhattacharjee S, van Ooij C, 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    Bhattacharjee, S.2    van Ooij, C.3
  • 22
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti M, Good RT, Rug 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    Good, R.T.2    Rug, M.3
  • 23
    • 33751104451 scopus 로고    scopus 로고
    • Common infection strategies of pathogenic eukaryotes
    • Haldar K, Kamoun S, Hiller NL, et al. Common infection strategies of pathogenic eukaryotes. Nat Rev Microbiol 2006; 4:922-931.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 922-931
    • Haldar, K.1    Kamoun, S.2    Hiller, N.L.3
  • 24
    • 9144258616 scopus 로고    scopus 로고
    • Protein kinases of the human malaria parasite Plasmodium falciparum: The kinome of a divergent eukaryote
    • Ward P, Equinet L, Packer J, Doerig C. Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics 2004; 5:79.
    • (2004) BMC Genomics , vol.5 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 25
    • 3042516019 scopus 로고    scopus 로고
    • A Plasmodium gene family encoding Maurer's cleft membrane proteins: Structural properties and expression profiling
    • Sam-Yellowe TY, Florens L, Johnson JR, et al. A Plasmodium gene family encoding Maurer's cleft membrane proteins: structural properties and expression profiling. Genome Res 2004; 14:1052-1059.
    • (2004) Genome Res , vol.14 , pp. 1052-1059
    • Sam-Yellowe, T.Y.1    Florens, L.2    Johnson, J.R.3
  • 26
    • 23644449843 scopus 로고    scopus 로고
    • A new Apicomplexa-specific protein kinase family: Multiple members in Plasmodium falciparum, all with an export signature
    • Schneider AG, Mercereau-Puijalon O. A new Apicomplexa-specific protein kinase family: multiple members in Plasmodium falciparum, all with an export signature. BMC Genomics 2005; 6:30.
    • (2005) BMC Genomics , vol.6 , pp. 30
    • Schneider, A.G.1    Mercereau-Puijalon, O.2
  • 27
    • 33646926281 scopus 로고    scopus 로고
    • Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites
    • Sargeant TJ, Marti M, Caler E, 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    Marti, M.2    Caler, E.3
  • 28
    • 84886944529 scopus 로고    scopus 로고
    • A Plasmodium whole-genome synteny map: Indels and synteny breakpoints as foci for species-specific genes
    • Kooij TW, Carlton JM, Bidwell SL, et al. A Plasmodium whole-genome synteny map: indels and synteny breakpoints as foci for species-specific genes. PLoS Pathog 2005; 1:e44.
    • (2005) PLoS Pathog , vol.1
    • Kooij, T.W.1    Carlton, J.M.2    Bidwell, S.L.3
  • 29
    • 33646906197 scopus 로고    scopus 로고
    • The malarial host-targeting signal is conserved in the Irish potato famine pathogen
    • The work provides evidence that diverse pathogenic euakryotes such as malaria parasites and oomycetes can use functionally equivalent signals to secrete effectors in to vastly different hosts such as erythrocytes and plant cells
    • Bhattacharjee S, Hiller NL, Liolios K, et al. The malarial host-targeting signal is conserved in the Irish potato famine pathogen. PLoS Pathog 2006; 2:e50. The work provides evidence that diverse pathogenic euakryotes such as malaria parasites and oomycetes can use functionally equivalent signals to secrete effectors in to vastly different hosts such as erythrocytes and plant cells.
    • (2006) PLoS Pathog , vol.2
    • Bhattacharjee, S.1    Hiller, N.L.2    Liolios, K.3
  • 30
    • 0345257824 scopus 로고    scopus 로고
    • Characterization of the pathway for transport of the cytoadherence-mediating protein, PfEMP1, to the host cell surface in malaria parasite-infected erythrocytes
    • 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 2003; 50:1215-1227.
    • (2003) Mol Microbiol , vol.50 , pp. 1215-1227
    • Kriek, N.1    Tilley, L.2    Horrocks, P.3
  • 31
    • 33644895382 scopus 로고    scopus 로고
    • Cooke BM, Buckingham DW, Glenister FK, 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. This study utilizes a genetic knockout to show that a single parasite protein regulates transport of the virulence adhesin PfEMP1 from intraerythrocytic 'cleft' intermediates to the erythrocyte surface.
    • Cooke BM, Buckingham DW, Glenister FK, 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. This study utilizes a genetic knockout to show that a single parasite protein regulates transport of the virulence adhesin PfEMP1 from intraerythrocytic 'cleft' intermediates to the erythrocyte surface.
  • 32
    • 0033982042 scopus 로고    scopus 로고
    • Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes
    • Trelka DP, Schneider TG, Reeder JC, Taraschi TF. Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes. Mol Biochem Parasitol 2000; 106:131-145.
    • (2000) Mol Biochem Parasitol , vol.106 , pp. 131-145
    • Trelka, D.P.1    Schneider, T.G.2    Reeder, J.C.3    Taraschi, T.F.4
  • 33
    • 0142008046 scopus 로고    scopus 로고
    • Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites
    • Taraschi TF, O'Donnell M, Martinez S, et al. Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites. Blood 2003; 102:3420-3426.
    • (2003) Blood , vol.102 , pp. 3420-3426
    • Taraschi, T.F.1    O'Donnell, M.2    Martinez, S.3
  • 34
    • 18544374027 scopus 로고    scopus 로고
    • Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes
    • Knuepfer E, Rug M, Klonis N, et al. Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes. Blood 2005; 105:4078-4087.
    • (2005) Blood , vol.105 , pp. 4078-4087
    • Knuepfer, E.1    Rug, M.2    Klonis, N.3
  • 35
    • 14544288184 scopus 로고    scopus 로고
    • A potential novel mechanism for the insertion of a membrane protein revealed by a biochemical analysis of the Plasmodium falciparum cytoadherence molecule PfEMP-1
    • Papakrivos J, Newbold CI, 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 2005; 55:1272-1284.
    • (2005) Mol Microbiol , vol.55 , pp. 1272-1284
    • Papakrivos, J.1    Newbold, C.I.2    Lingelbach, K.3
  • 36
    • 0034778404 scopus 로고    scopus 로고
    • Evidence for a role for a Plasmodium falciparum homologue of Sec31p in the export of proteins to the surface of malaria parasite-infected erythrocytes
    • Adisa A, Albano FR, Reeder J, et al. 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 2001; 114 (Pt 18):3377-3386.
    • (2001) J Cell Sci , vol.114 , Issue.PART 18 , pp. 3377-3386
    • Adisa, A.1    Albano, F.R.2    Reeder, J.3
  • 37
    • 0032855341 scopus 로고    scopus 로고
    • A homologue of Sar1p localizes to a novel trafficking pathway in malaria-infected erythrocytes
    • Albano FR, Berman A, La Greca N, et al. A homologue of Sar1p localizes to a novel trafficking pathway in malaria-infected erythrocytes. Eur J Cell Biol 1999; 78:453-462.
    • (1999) Eur J Cell Biol , vol.78 , pp. 453-462
    • Albano, F.R.1    Berman, A.2    La Greca, N.3
  • 38
    • 0035805639 scopus 로고    scopus 로고
    • 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
    • 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 2001; 276:15249-15255.
    • (2001) J Biol Chem , vol.276 , pp. 15249-15255
    • Hayashi, M.1    Taniguchi, S.2    Ishizuka, Y.3
  • 39
    • 0041940227 scopus 로고    scopus 로고
    • Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells
    • Waller KL, Nunomura W, An X, et al. Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells. Blood 2003; 102:1911-1914.
    • (2003) Blood , vol.102 , pp. 1911-1914
    • Waller, K.L.1    Nunomura, W.2    An, X.3
  • 40
    • 0037040201 scopus 로고    scopus 로고
    • Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum
    • Banumathy G, Singh V, Tatu U. Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum. J Biol Chem 2002; 277:3902-3912.
    • (2002) J Biol Chem , vol.277 , pp. 3902-3912
    • Banumathy, G.1    Singh, V.2    Tatu, U.3
  • 41
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan CY, Lee S, Cyr DM. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 2003; 8:309-316.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 42
    • 0037474121 scopus 로고    scopus 로고
    • Dissecting apicoplast targeting in the malaria parasite Plasmodium falciparum
    • Foth BJ, Ralph SA, Tonkin CJ, et al. Dissecting apicoplast targeting in the malaria parasite Plasmodium falciparum. Science 2003; 299:705-708.
    • (2003) Science , vol.299 , pp. 705-708
    • Foth, B.J.1    Ralph, S.A.2    Tonkin, C.J.3
  • 43
    • 1642602656 scopus 로고    scopus 로고
    • Differentiating the pathologies of cerebral malaria by postmortem parasite counts
    • Taylor TE, Fu WJ, Carr RA, et al. Differentiating the pathologies of cerebral malaria by postmortem parasite counts. Nat Med 2004; 10:143-145.
    • (2004) Nat Med , vol.10 , pp. 143-145
    • Taylor, T.E.1    Fu, W.J.2    Carr, R.A.3
  • 44
    • 33947356275 scopus 로고    scopus 로고
    • Malaria: Mechanisms of erythrocytic infection and pathological correlates of severe disease
    • Haldar K, Murphy S, Miller D, Taylor T. Malaria: Mechanisms of erythrocytic infection and pathological correlates of severe disease. Annu Rev Pathol 2007; 2:217-249.
    • (2007) Annu Rev Pathol , vol.2 , pp. 217-249
    • Haldar, K.1    Murphy, S.2    Miller, D.3    Taylor, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.