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Volumn 8, Issue 4, 2013, Pages

Life Cycle-Dependent Cytoskeletal Modifications in Plasmodium falciparum Infected Erythrocytes

Author keywords

[No Author keywords available]

Indexed keywords

KNOB ASSOCIATED HISTIDINE PROTEIN; PROTOZOAL PROTEIN; QUANTUM DOT; SPECTRIN; TETRAMER; UNCLASSIFIED DRUG;

EID: 84876041398     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0061170     Document Type: Article
Times cited : (55)

References (37)
  • 2
    • 0035191853 scopus 로고    scopus 로고
    • The malaria-infected red blood cell: structural and functional changes
    • Cooke BM, Mohandas N, Coppel RL, (2001) The malaria-infected red blood cell: structural and functional changes. Adv Parasitol 50: 1-86.
    • (2001) Adv Parasitol , vol.50 , pp. 1-86
    • Cooke, B.M.1    Mohandas, N.2    Coppel, R.L.3
  • 3
    • 0024382452 scopus 로고
    • Abnormalities in the mechanical properties of red blood cells caused by Plasmodium falciparum
    • Nash GB, O'Brien E, Gordon-Smith EC, Dormandy JA, (1989) Abnormalities in the mechanical properties of red blood cells caused by Plasmodium falciparum. Blood 74: 855-861.
    • (1989) Blood , vol.74 , pp. 855-861
    • Nash, G.B.1    O'Brien, E.2    Gordon-Smith, E.C.3    Dormandy, J.A.4
  • 4
    • 0030910143 scopus 로고    scopus 로고
    • Erythrocyte membrane alterations in Plasmodium falciparum malaria sequestration
    • Oh SS, Chishti AH, Palek J, Liu SC, (1997) Erythrocyte membrane alterations in Plasmodium falciparum malaria sequestration. Curr Opin Hematol 4: 148-154.
    • (1997) Curr Opin Hematol , vol.4 , pp. 148-154
    • Oh, S.S.1    Chishti, A.H.2    Palek, J.3    Liu, S.C.4
  • 5
    • 24744459649 scopus 로고    scopus 로고
    • Structural and functional studies of interaction between Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin
    • Pei X, An X, Guo X, Tarnawski M, Coppel R, et al. (2005) Structural and functional studies of interaction between Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin. J Biol Chem 280: 31166-31171.
    • (2005) J Biol Chem , vol.280 , pp. 31166-31171
    • Pei, X.1    An, X.2    Guo, X.3    Tarnawski, M.4    Coppel, R.5
  • 6
    • 34247123673 scopus 로고    scopus 로고
    • Spectrin-based skeleton in red blood cells and malaria
    • Dhermy D, Schrevel J, Lecomte MC, (2007) Spectrin-based skeleton in red blood cells and malaria. Curr Opin Hematol 14: 198-202.
    • (2007) Curr Opin Hematol , vol.14 , pp. 198-202
    • Dhermy, D.1    Schrevel, J.2    Lecomte, M.C.3
  • 7
    • 0023915893 scopus 로고
    • Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis
    • Waugh RE, Agre P, (1988) Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis. J Clin Invest 81: 133-141.
    • (1988) J Clin Invest , vol.81 , pp. 133-141
    • Waugh, R.E.1    Agre, P.2
  • 8
    • 0033553410 scopus 로고    scopus 로고
    • Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton
    • Le Bonniec S, Deregnaucourt C, Redeker V, Banerjee R, Grellier P, et al. (1999) Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton. J Biol Chem 274: 14218-14223.
    • (1999) J Biol Chem , vol.274 , pp. 14218-14223
    • Le Bonniec, S.1    Deregnaucourt, C.2    Redeker, V.3    Banerjee, R.4    Grellier, P.5
  • 9
    • 0033745048 scopus 로고    scopus 로고
    • A cysteine protease activity from Plasmodium falciparum cleaves human erythrocyte ankyrin
    • Raphael P, Takakuwa Y, Manno S, Liu SC, Chishti AH, et al. (2000) A cysteine protease activity from Plasmodium falciparum cleaves human erythrocyte ankyrin. Mol Biochem Parasitol 110: 259-272.
    • (2000) Mol Biochem Parasitol , vol.110 , pp. 259-272
    • Raphael, P.1    Takakuwa, Y.2    Manno, S.3    Liu, S.C.4    Chishti, A.H.5
  • 10
    • 0036682503 scopus 로고    scopus 로고
    • Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development
    • Hanspal M, Dua M, Takakuwa Y, Chishti AH, Mizuno A, (2002) Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development. Blood 100: 1048-1054.
    • (2002) Blood , vol.100 , pp. 1048-1054
    • Hanspal, M.1    Dua, M.2    Takakuwa, Y.3    Chishti, A.H.4    Mizuno, A.5
  • 11
    • 0036183460 scopus 로고    scopus 로고
    • Hydrolysis of erythrocyte proteins by proteases of malaria parasites
    • Rosenthal PJ, (2002) Hydrolysis of erythrocyte proteins by proteases of malaria parasites. Curr Opin Hematol 9: 140-145.
    • (2002) Curr Opin Hematol , vol.9 , pp. 140-145
    • Rosenthal, P.J.1
  • 12
    • 65649112111 scopus 로고    scopus 로고
    • Apicomplexan parasites co-opt host calpains to facilitate their escape from infected cells
    • Chandramohanadas R, Davis PH, Beiting DP, Harbut MB, Darling C, et al. (2009) Apicomplexan parasites co-opt host calpains to facilitate their escape from infected cells. Science 324: 794-797.
    • (2009) Science , vol.324 , pp. 794-797
    • Chandramohanadas, R.1    Davis, P.H.2    Beiting, D.P.3    Harbut, M.B.4    Darling, C.5
  • 13
    • 0031958201 scopus 로고    scopus 로고
    • Structure of the erythrocyte membrane skeleton as observed by atomic force microscopy
    • Takeuchi M, Miyamoto H, Sako Y, Komizu H, Kusumi A, (1998) Structure of the erythrocyte membrane skeleton as observed by atomic force microscopy. Biophys J 74: 2171-2183.
    • (1998) Biophys J , vol.74 , pp. 2171-2183
    • Takeuchi, M.1    Miyamoto, H.2    Sako, Y.3    Komizu, H.4    Kusumi, A.5
  • 15
    • 2142845951 scopus 로고    scopus 로고
    • Sample preparation and imaging of erythrocyte cytoskeleton with the atomic force microscopy
    • Liu F, Burgess J, Mizukami H, Ostafin A, (2003) Sample preparation and imaging of erythrocyte cytoskeleton with the atomic force microscopy. Cell Biochem Biophys 38: 251-270.
    • (2003) Cell Biochem Biophys , vol.38 , pp. 251-270
    • Liu, F.1    Burgess, J.2    Mizukami, H.3    Ostafin, A.4
  • 16
    • 0031193934 scopus 로고    scopus 로고
    • Imaging Plasmodium falciparum-infected ghost and parasite by atomic force microscopy
    • Garcia CR, Takeuschi M, Yoshioka K, Miyamoto H, (1997) Imaging Plasmodium falciparum-infected ghost and parasite by atomic force microscopy. J Struct Biol 119: 92-98.
    • (1997) J Struct Biol , vol.119 , pp. 92-98
    • Garcia, C.R.1    Takeuschi, M.2    Yoshioka, K.3    Miyamoto, H.4
  • 18
    • 33745963537 scopus 로고    scopus 로고
    • Observations on the internal and surface morphology of malaria infected blood cells using optical and atomic force microscopy
    • Li A, Mansoor AH, Tan KS, Lim CT, (2006) Observations on the internal and surface morphology of malaria infected blood cells using optical and atomic force microscopy. J Microbiol Methods 66: 434-439.
    • (2006) J Microbiol Methods , vol.66 , pp. 434-439
    • Li, A.1    Mansoor, A.H.2    Tan, K.S.3    Lim, C.T.4
  • 19
    • 0023430419 scopus 로고
    • Plasmodium falciparum: fine structural changes in the cytoskeletons of infected erythrocytes
    • Taylor DW, Parra M, Stearns ME, (1987) Plasmodium falciparum: fine structural changes in the cytoskeletons of infected erythrocytes. Exp Parasitol 64: 178-187.
    • (1987) Exp Parasitol , vol.64 , pp. 178-187
    • Taylor, D.W.1    Parra, M.2    Stearns, M.E.3
  • 20
    • 83055168540 scopus 로고    scopus 로고
    • The malaria parasite progressively dismantles the host erythrocyte cytoskeleton for efficient egress
    • Millholland MG, Chandramohanadas R, Pizzarro A, Wehr A, Shi H, et al. (2011) The malaria parasite progressively dismantles the host erythrocyte cytoskeleton for efficient egress. Mol Cell Proteomics 10:M111 010678.
    • (2011) Mol Cell Proteomics , vol.10
    • Millholland, M.G.1    Chandramohanadas, R.2    Pizzarro, A.3    Wehr, A.4    Shi, H.5
  • 21
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers TJ, Branton D, (1985) Visualization of the protein associations in the erythrocyte membrane skeleton. Proc Natl Acad Sci U S A 82: 6153-6157.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 22
    • 0025284142 scopus 로고
    • On the structure of erythrocyte spectrin in partially expanded membrane skeletons
    • McGough AM, Josephs R, (1990) On the structure of erythrocyte spectrin in partially expanded membrane skeletons. Proc Natl Acad Sci U S A 87: 5208-5212.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5208-5212
    • McGough, A.M.1    Josephs, R.2
  • 23
    • 81255184413 scopus 로고    scopus 로고
    • Native ultrastructure of the red cell cytoskeleton by cryo-electron tomography
    • Nans A, Mohandas N, Stokes DL, (2011) Native ultrastructure of the red cell cytoskeleton by cryo-electron tomography. Biophys J 101: 2341-2350.
    • (2011) Biophys J , vol.101 , pp. 2341-2350
    • Nans, A.1    Mohandas, N.2    Stokes, D.L.3
  • 24
    • 0026570819 scopus 로고
    • Repeat structures in a Plasmodium falciparum protein (MESA) that binds human erythrocyte protein 4.1
    • Coppel RL, (1992) Repeat structures in a Plasmodium falciparum protein (MESA) that binds human erythrocyte protein 4.1. Mol Biochem Parasitol 50: 335-347.
    • (1992) Mol Biochem Parasitol , vol.50 , pp. 335-347
    • Coppel, R.L.1
  • 25
    • 34249887606 scopus 로고    scopus 로고
    • Effect of plasmodial RESA protein on deformability of human red blood cells harboring Plasmodium falciparum
    • Mills JP, Diez-Silva M, Quinn DJ, Dao M, Lang MJ, et al. (2007) Effect of plasmodial RESA protein on deformability of human red blood cells harboring Plasmodium falciparum. Proc Natl Acad Sci U S A 104: 9213-9217.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9213-9217
    • Mills, J.P.1    Diez-Silva, M.2    Quinn, D.J.3    Dao, M.4    Lang, M.J.5
  • 26
    • 0036464653 scopus 로고    scopus 로고
    • Contribution of parasite proteins to altered mechanical properties of malaria-infected red blood cells
    • Glenister FK, Coppel RL, Cowman AF, Mohandas N, Cooke BM, (2002) Contribution of parasite proteins to altered mechanical properties of malaria-infected red blood cells. Blood 99: 1060-1063.
    • (2002) Blood , vol.99 , pp. 1060-1063
    • Glenister, F.K.1    Coppel, R.L.2    Cowman, A.F.3    Mohandas, N.4    Cooke, B.M.5
  • 27
    • 0037200093 scopus 로고    scopus 로고
    • Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane
    • An X, Lecomte MC, Chasis JA, Mohandas N, Gratzer W, (2002) Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane. J Biol Chem 277: 31796-31800.
    • (2002) J Biol Chem , vol.277 , pp. 31796-31800
    • An, X.1    Lecomte, M.C.2    Chasis, J.A.3    Mohandas, N.4    Gratzer, W.5
  • 28
    • 0035238098 scopus 로고    scopus 로고
    • New insights into red cell network structure, elasticity, and spectrin unfolding--a current review
    • Discher DE, Carl P, (2001) New insights into red cell network structure, elasticity, and spectrin unfolding--a current review. Cell Mol Biol Lett 6: 593-606.
    • (2001) Cell Mol Biol Lett , vol.6 , pp. 593-606
    • Discher, D.E.1    Carl, P.2
  • 29
    • 0027495907 scopus 로고
    • Membrane rigidity of red blood cells parasitized by different strains of Plasmodium falciparum
    • Paulitschke M, Nash GB, (1993) Membrane rigidity of red blood cells parasitized by different strains of Plasmodium falciparum. J Lab Clin Med 122: 581-589.
    • (1993) J Lab Clin Med , vol.122 , pp. 581-589
    • Paulitschke, M.1    Nash, G.B.2
  • 30
    • 0021350185 scopus 로고
    • Plasmodium falciparum maturation abolishes physiologic red cell deformability
    • Cranston HA, Boylan CW, Carroll GL, Sutera SP, Williamson JR, et al. (1984) Plasmodium falciparum maturation abolishes physiologic red cell deformability. Science 223: 400-403.
    • (1984) Science , vol.223 , pp. 400-403
    • Cranston, H.A.1    Boylan, C.W.2    Carroll, G.L.3    Sutera, S.P.4    Williamson, J.R.5
  • 32
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W, Jensen JB, (1976) Human malaria parasites in continuous culture. Science 193: 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 33
  • 34
    • 15044345186 scopus 로고    scopus 로고
    • Plasmodium falciparum: a simplified technique for obtaining singly infected erythrocytes
    • Puthia MK, Tan KS, (2005) Plasmodium falciparum: a simplified technique for obtaining singly infected erythrocytes. Parasitol Res 95: 176-178.
    • (2005) Parasitol Res , vol.95 , pp. 176-178
    • Puthia, M.K.1    Tan, K.S.2
  • 35
    • 2942525658 scopus 로고    scopus 로고
    • One-step concentration of malarial parasite-infected red blood cells and removal of contaminating white blood cells
    • Trang DT, Huy NT, Kariu T, Tajima K, Kamei K, (2004) One-step concentration of malarial parasite-infected red blood cells and removal of contaminating white blood cells. Malar J 3: 7.
    • (2004) Malar J , vol.3 , pp. 7
    • Trang, D.T.1    Huy, N.T.2    Kariu, T.3    Tajima, K.4    Kamei, K.5
  • 36
    • 0023225664 scopus 로고
    • Plasmodium species: flow cytometry and microfluorometry assessments of DNA content and synthesis
    • Janse CJ, van Vianen PH, Tanke HJ, Mons B, Ponnudurai T, et al. (1987) Plasmodium species: flow cytometry and microfluorometry assessments of DNA content and synthesis. Exp Parasitol 64: 88-94.
    • (1987) Exp Parasitol , vol.64 , pp. 88-94
    • Janse, C.J.1    van Vianen, P.H.2    Tanke, H.J.3    Mons, B.4    Ponnudurai, T.5
  • 37
    • 58649116882 scopus 로고    scopus 로고
    • Immune atomic force microscopy of prestin-transfected CHO cells using quantum dots
    • Murakoshi M, Iida K, Kumano S, Wada H, (2009) Immune atomic force microscopy of prestin-transfected CHO cells using quantum dots. Pflugers Arch 457: 885-898.
    • (2009) Pflugers Arch , vol.457 , pp. 885-898
    • Murakoshi, M.1    Iida, K.2    Kumano, S.3    Wada, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.