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Volumn 24, Issue 5, 2008, Pages 210-218

Hot, sweet and sticky: the glycobiology of Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; GLYCOCONJUGATE; GLYCOLYTIC ENZYME; GLYCOSYLATED PROTEIN; INOSITOL DERIVATIVE; LECTIN; MEMBRANE PROTEIN;

EID: 42749094919     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2008.02.007     Document Type: Review
Times cited : (59)

References (74)
  • 1
    • 28444489661 scopus 로고    scopus 로고
    • Role of surfactant protein D (SP-D) in innate immunity in the gastric mucosa: evidence of interaction with Helicobacter pylori lipopolysaccharide
    • Moran A.P., et al. Role of surfactant protein D (SP-D) in innate immunity in the gastric mucosa: evidence of interaction with Helicobacter pylori lipopolysaccharide. J. Endotoxin Res. 11 (2005) 357-362
    • (2005) J. Endotoxin Res. , vol.11 , pp. 357-362
    • Moran, A.P.1
  • 2
    • 36749056771 scopus 로고    scopus 로고
    • The war against influenza: discovery and development of sialidase inhibitors
    • von Itzstein M. The war against influenza: discovery and development of sialidase inhibitors. Nat. Rev. Drug Discov. 6 (2007) 967-974
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 967-974
    • von Itzstein, M.1
  • 3
    • 33747853193 scopus 로고    scopus 로고
    • Enlistment of omics technologies in the fight against malaria: Panacea or Pandora's Box?
    • Hayes C.N., et al. Enlistment of omics technologies in the fight against malaria: Panacea or Pandora's Box?. J. Pestic. Sci. 31 (2006) 263-272
    • (2006) J. Pestic. Sci. , vol.31 , pp. 263-272
    • Hayes, C.N.1
  • 4
    • 25844527419 scopus 로고    scopus 로고
    • Protozoan parasite-specific carbohydrate structures
    • Mendonça-Previato L., et al. Protozoan parasite-specific carbohydrate structures. Curr. Opin. Struct. Biol. 15 (2005) 499-505
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 499-505
    • Mendonça-Previato, L.1
  • 5
    • 0032582846 scopus 로고    scopus 로고
    • A novel multi-domain mucin-like glycoprotein of Cryptosporidium parvum mediates invasion
    • Barnes D.A., et al. A novel multi-domain mucin-like glycoprotein of Cryptosporidium parvum mediates invasion. Mol. Biochem. Parasitol. 96 (1998) 93-110
    • (1998) Mol. Biochem. Parasitol. , vol.96 , pp. 93-110
    • Barnes, D.A.1
  • 6
    • 13444281918 scopus 로고    scopus 로고
    • The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases
    • Samuelson J., et al. The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1548-1553
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1548-1553
    • Samuelson, J.1
  • 8
    • 0031726220 scopus 로고    scopus 로고
    • Metabolic changes of the malaria parasite during the transition from the human to the mosquito host
    • Lang-Unnasch N., and Murphy A.D. Metabolic changes of the malaria parasite during the transition from the human to the mosquito host. Annu. Rev. Microbiol. 52 (1998) 561-590
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 561-590
    • Lang-Unnasch, N.1    Murphy, A.D.2
  • 9
    • 42749083654 scopus 로고    scopus 로고
    • Molecular approaches to malaria: glycolysis in asexual-stage parasites
    • Sherman I.W. (Ed), ASM Press
    • Woodrow C., and Krishna S. Molecular approaches to malaria: glycolysis in asexual-stage parasites. In: Sherman I.W. (Ed). Molecular Approaches to Malaria (2005), ASM Press 223-233
    • (2005) Molecular Approaches to Malaria , pp. 223-233
    • Woodrow, C.1    Krishna, S.2
  • 10
    • 0037015602 scopus 로고    scopus 로고
    • A proteomic view of the Plasmodium falciparum life cycle
    • Florens L., et al. A proteomic view of the Plasmodium falciparum life cycle. Nature 419 (2002) 520-526
    • (2002) Nature , vol.419 , pp. 520-526
    • Florens, L.1
  • 11
    • 0030294274 scopus 로고    scopus 로고
    • The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design
    • Dunn C.R., et al. The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design. Nat. Struct. Biol. 3 (1996) 912-915
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 912-915
    • Dunn, C.R.1
  • 12
    • 3843112304 scopus 로고    scopus 로고
    • Identification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity
    • Cameron A., et al. Identification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity. J. Biol. Chem. 279 (2004) 31429-31439
    • (2004) J. Biol. Chem. , vol.279 , pp. 31429-31439
    • Cameron, A.1
  • 13
    • 33645306878 scopus 로고    scopus 로고
    • A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites
    • Baum J., et al. A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J. Biol. Chem. 281 (2006) 5197-5208
    • (2006) J. Biol. Chem. , vol.281 , pp. 5197-5208
    • Baum, J.1
  • 14
    • 0031050860 scopus 로고    scopus 로고
    • Efflux of 6-deoxy-D-glucose from Plasmodium falciparum-infected erythrocytes via two saturable carriers
    • Goodyer I.D., et al. Efflux of 6-deoxy-D-glucose from Plasmodium falciparum-infected erythrocytes via two saturable carriers. Mol. Biochem. Parasitol. 84 (1997) 229-239
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 229-239
    • Goodyer, I.D.1
  • 15
    • 0034730173 scopus 로고    scopus 로고
    • Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes
    • Woodrow C.J., et al. Hexose permeation pathways in Plasmodium falciparum-infected erythrocytes. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9931-9936
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9931-9936
    • Woodrow, C.J.1
  • 16
    • 4344610676 scopus 로고    scopus 로고
    • Analysis of Plasmodium vivax hexose transporters and effects of a parasitocidal inhibitor
    • Joet T., et al. Analysis of Plasmodium vivax hexose transporters and effects of a parasitocidal inhibitor. Biochem. J. 381 (2004) 905-909
    • (2004) Biochem. J. , vol.381 , pp. 905-909
    • Joet, T.1
  • 17
    • 0037934729 scopus 로고    scopus 로고
    • Validation of the hexose transporter of Plasmodium falciparum as a novel drug target
    • Joet T., et al. Validation of the hexose transporter of Plasmodium falciparum as a novel drug target. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7476-7479
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7476-7479
    • Joet, T.1
  • 18
    • 33745453189 scopus 로고    scopus 로고
    • Membrane transporters in the relict plastid of malaria parasites
    • Mullin K.A., et al. Membrane transporters in the relict plastid of malaria parasites. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 9572-9577
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9572-9577
    • Mullin, K.A.1
  • 19
    • 0033984166 scopus 로고    scopus 로고
    • More on protein glycosylation in the malaria parasite
    • Kimura E.A., et al. More on protein glycosylation in the malaria parasite. Parasitol. Today 16 (2000) 38-40
    • (2000) Parasitol. Today , vol.16 , pp. 38-40
    • Kimura, E.A.1
  • 20
    • 0033118395 scopus 로고    scopus 로고
    • Protein glycosylation in the malaria parasite
    • Gowda D.C., and Davidson E.A. Protein glycosylation in the malaria parasite. Parasitol. Today 15 (1999) 147-152
    • (1999) Parasitol. Today , vol.15 , pp. 147-152
    • Gowda, D.C.1    Davidson, E.A.2
  • 22
    • 0030932207 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors represent the major carbohydrate modification in proteins of intraerythrocytic stage Plasmodium falciparum
    • Gowda D.C., et al. Glycosylphosphatidylinositol anchors represent the major carbohydrate modification in proteins of intraerythrocytic stage Plasmodium falciparum. J. Biol. Chem. 272 (1997) 6428-6439
    • (1997) J. Biol. Chem. , vol.272 , pp. 6428-6439
    • Gowda, D.C.1
  • 23
    • 0036591274 scopus 로고    scopus 로고
    • Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system
    • Kedees M.H., et al. Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system. Exp. Parasitol. 101 (2002) 64-68
    • (2002) Exp. Parasitol. , vol.101 , pp. 64-68
    • Kedees, M.H.1
  • 24
    • 0034074496 scopus 로고    scopus 로고
    • Plasmodium falciparum: merozoite surface proteins 1 and 2 are not posttranslationally modified by classical N- or O-glycans
    • Berhe S., et al. Plasmodium falciparum: merozoite surface proteins 1 and 2 are not posttranslationally modified by classical N- or O-glycans. Exp. Parasitol. 94 (2000) 194-197
    • (2000) Exp. Parasitol. , vol.94 , pp. 194-197
    • Berhe, S.1
  • 25
    • 33746273843 scopus 로고    scopus 로고
    • Identification and stoichiometry of glycosylphosphatidylinositol-anchored membrane proteins of the human malaria parasite Plasmodium falciparum
    • Gilson P.R., et al. Identification and stoichiometry of glycosylphosphatidylinositol-anchored membrane proteins of the human malaria parasite Plasmodium falciparum. Mol. Cell. Proteomics 5 (2006) 1286-1299
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1286-1299
    • Gilson, P.R.1
  • 26
    • 0028086445 scopus 로고
    • Glycosylphosphatidylinositols synthesized by asexual erythrocytic stages of the malarial parasite, Plasmodium falciparum. Candidates for plasmodial glycosylphosphatidylinositol membrane anchor precursors and pathogenicity factors
    • Gerold P., et al. Glycosylphosphatidylinositols synthesized by asexual erythrocytic stages of the malarial parasite, Plasmodium falciparum. Candidates for plasmodial glycosylphosphatidylinositol membrane anchor precursors and pathogenicity factors. J. Biol. Chem. 269 (1994) 2597-2606
    • (1994) J. Biol. Chem. , vol.269 , pp. 2597-2606
    • Gerold, P.1
  • 27
    • 0033572840 scopus 로고    scopus 로고
    • Biosynthesis of glycosylphosphatidylinositols of Plasmodium falciparum in a cell-free incubation system: inositol acylation is needed for mannosylation of glycosylphosphatidylinositols
    • Gerold P., et al. Biosynthesis of glycosylphosphatidylinositols of Plasmodium falciparum in a cell-free incubation system: inositol acylation is needed for mannosylation of glycosylphosphatidylinositols. Biochem. J. 344 (1999) 731-738
    • (1999) Biochem. J. , vol.344 , pp. 731-738
    • Gerold, P.1
  • 28
    • 0036070685 scopus 로고    scopus 로고
    • Genes for glycosylphosphatidylinositol toxin biosynthesis in Plasmodium falciparum
    • Delorenzi M., et al. Genes for glycosylphosphatidylinositol toxin biosynthesis in Plasmodium falciparum. Infect. Immun. 70 (2002) 4510-4522
    • (2002) Infect. Immun. , vol.70 , pp. 4510-4522
    • Delorenzi, M.1
  • 29
    • 0026795458 scopus 로고
    • The basolateral domain of the hepatocyte plasma membrane bears receptors for the circumsporozoite protein of Plasmodium falciparum sporozoites
    • Cerami C., et al. The basolateral domain of the hepatocyte plasma membrane bears receptors for the circumsporozoite protein of Plasmodium falciparum sporozoites. Cell 70 (1992) 1021-1033
    • (1992) Cell , vol.70 , pp. 1021-1033
    • Cerami, C.1
  • 30
    • 0026642642 scopus 로고
    • Binding of malarial circumsporozoite protein to sulfatides [Gal(3-SO4)beta 1-Cer] and cholesterol-3-sulfate and its dependence on disulfide bond formation between cysteines in region II
    • Cerami C., et al. Binding of malarial circumsporozoite protein to sulfatides [Gal(3-SO4)beta 1-Cer] and cholesterol-3-sulfate and its dependence on disulfide bond formation between cysteines in region II. Mol. Biochem. Parasitol. 54 (1992) 1-12
    • (1992) Mol. Biochem. Parasitol. , vol.54 , pp. 1-12
    • Cerami, C.1
  • 31
    • 0027457377 scopus 로고
    • Malaria circumsporozoite protein binds to heparan sulfate proteoglycans associated with the surface membrane of hepatocytes
    • Frevert U., et al. Malaria circumsporozoite protein binds to heparan sulfate proteoglycans associated with the surface membrane of hepatocytes. J. Exp. Med. 177 (1993) 1287-1298
    • (1993) J. Exp. Med. , vol.177 , pp. 1287-1298
    • Frevert, U.1
  • 32
    • 0026716363 scopus 로고
    • Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates
    • Pancake S.J., et al. Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates. J. Cell Biol. 117 (1992) 1351-1357
    • (1992) J. Cell Biol. , vol.117 , pp. 1351-1357
    • Pancake, S.J.1
  • 33
    • 0030745648 scopus 로고    scopus 로고
    • TRAP is necessary for gliding motility and infectivity of plasmodium sporozoites
    • Sultan A.A., et al. TRAP is necessary for gliding motility and infectivity of plasmodium sporozoites. Cell 90 (1997) 511-522
    • (1997) Cell , vol.90 , pp. 511-522
    • Sultan, A.A.1
  • 34
    • 0027326632 scopus 로고
    • Thrombospondin related anonymous protein (TRAP) of Plasmodium falciparum binds specifically to sulfated glycoconjugates and to HepG2 hepatoma cells suggesting a role for this molecule in sporozoite invasion of hepatocytes
    • Muller H.M., et al. Thrombospondin related anonymous protein (TRAP) of Plasmodium falciparum binds specifically to sulfated glycoconjugates and to HepG2 hepatoma cells suggesting a role for this molecule in sporozoite invasion of hepatocytes. EMBO J. 12 (1993) 2881-2889
    • (1993) EMBO J. , vol.12 , pp. 2881-2889
    • Muller, H.M.1
  • 35
    • 2542527673 scopus 로고    scopus 로고
    • Structural and functional dissection of the adhesive domains of Plasmodium falciparum thrombospondin-related anonymous protein (TRAP)
    • Akhouri R.R., et al. Structural and functional dissection of the adhesive domains of Plasmodium falciparum thrombospondin-related anonymous protein (TRAP). Biochem. J. 379 (2004) 815-822
    • (2004) Biochem. J. , vol.379 , pp. 815-822
    • Akhouri, R.R.1
  • 36
    • 0028122878 scopus 로고
    • Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum
    • Sim B.K., et al. Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum. Science 264 (1994) 1941-1944
    • (1994) Science , vol.264 , pp. 1941-1944
    • Sim, B.K.1
  • 37
    • 0027282445 scopus 로고
    • N-acetylglucosamine-binding proteins on Plasmodium falciparum merozoite surface
    • el Moudni B., et al. N-acetylglucosamine-binding proteins on Plasmodium falciparum merozoite surface. Glycobiology 3 (1993) 305-312
    • (1993) Glycobiology , vol.3 , pp. 305-312
    • el Moudni, B.1
  • 38
    • 0022485907 scopus 로고
    • Surface Plasmodium sugar-binding components evidenced by fluorescent neoglycoproteins
    • Schrevel J., et al. Surface Plasmodium sugar-binding components evidenced by fluorescent neoglycoproteins. Biol. Cell 56 (1986) 49-55
    • (1986) Biol. Cell , vol.56 , pp. 49-55
    • Schrevel, J.1
  • 39
    • 0034691137 scopus 로고    scopus 로고
    • Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion
    • Reed M.B., et al. Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 7509-7514
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7509-7514
    • Reed, M.B.1
  • 40
    • 0037447273 scopus 로고    scopus 로고
    • Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways
    • Duraisingh M.T., et al. Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4796-4801
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4796-4801
    • Duraisingh, M.T.1
  • 41
    • 0033832193 scopus 로고    scopus 로고
    • Disruption of the C-terminal region of EBA-175 in the Dd2/Nm clone of Plasmodium falciparum does not affect erythrocyte invasion
    • Kaneko O., et al. Disruption of the C-terminal region of EBA-175 in the Dd2/Nm clone of Plasmodium falciparum does not affect erythrocyte invasion. Mol. Biochem. Parasitol. 110 (2000) 135-146
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 135-146
    • Kaneko, O.1
  • 42
    • 0027370205 scopus 로고
    • Evidence for two-stage binding by the 175-kD erythrocyte binding antigen of Plasmodium falciparum
    • Kain K.C., et al. Evidence for two-stage binding by the 175-kD erythrocyte binding antigen of Plasmodium falciparum. J. Exp. Med. 178 (1993) 1497-1505
    • (1993) J. Exp. Med. , vol.178 , pp. 1497-1505
    • Kain, K.C.1
  • 43
    • 22744456158 scopus 로고    scopus 로고
    • Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum
    • Tolia N.H., et al. Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum. Cell 122 (2005) 183-193
    • (2005) Cell , vol.122 , pp. 183-193
    • Tolia, N.H.1
  • 44
    • 0035191853 scopus 로고    scopus 로고
    • The malaria-infected red blood cell: structural and functional changes
    • Cooke B.M., et al. The malaria-infected red blood cell: structural and functional changes. Adv. Parasitol. 50 (2001) 1-86
    • (2001) Adv. Parasitol. , vol.50 , pp. 1-86
    • Cooke, B.M.1
  • 45
    • 35548954766 scopus 로고    scopus 로고
    • New approaches to pathogenesis of malaria in pregnancy
    • Rogerson S.J., and Boeuf P. New approaches to pathogenesis of malaria in pregnancy. Parasitology 134 (2007) 1883-1893
    • (2007) Parasitology , vol.134 , pp. 1883-1893
    • Rogerson, S.J.1    Boeuf, P.2
  • 46
    • 0029992826 scopus 로고    scopus 로고
    • Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta
    • Fried M., and Duffy P.E. Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta. Science 272 (1996) 1502-1504
    • (1996) Science , vol.272 , pp. 1502-1504
    • Fried, M.1    Duffy, P.E.2
  • 47
    • 33646022245 scopus 로고    scopus 로고
    • Plasmodium falciparum: chondroitin sulfate A is the major receptor for adhesion of parasitized erythrocytes in the placenta
    • Fried M., et al. Plasmodium falciparum: chondroitin sulfate A is the major receptor for adhesion of parasitized erythrocytes in the placenta. Exp. Parasitol. 113 (2006) 36-42
    • (2006) Exp. Parasitol. , vol.113 , pp. 36-42
    • Fried, M.1
  • 48
    • 0037151058 scopus 로고    scopus 로고
    • The structural motif in chondroitin sulfate for adhesion of Plasmodium falciparum-infected erythrocytes comprises disaccharide units of 4-O-sulfated and non-sulfated N-acetylgalactosamine linked to glucuronic acid
    • Chai W., et al. The structural motif in chondroitin sulfate for adhesion of Plasmodium falciparum-infected erythrocytes comprises disaccharide units of 4-O-sulfated and non-sulfated N-acetylgalactosamine linked to glucuronic acid. J. Biol. Chem. 277 (2002) 22438-22446
    • (2002) J. Biol. Chem. , vol.277 , pp. 22438-22446
    • Chai, W.1
  • 49
    • 0033954693 scopus 로고    scopus 로고
    • Adhesion of Plasmodium falciparum-infected erythrocytes to hyaluronic acid in placental malaria
    • Beeson J.G., et al. Adhesion of Plasmodium falciparum-infected erythrocytes to hyaluronic acid in placental malaria. Nat. Med. 6 (2000) 86-90
    • (2000) Nat. Med. , vol.6 , pp. 86-90
    • Beeson, J.G.1
  • 50
    • 17044371098 scopus 로고    scopus 로고
    • Broad analysis reveals a consistent pattern of var gene transcription in Plasmodium falciparum repeatedly selected for a defined adhesion phenotype
    • Duffy M.F., et al. Broad analysis reveals a consistent pattern of var gene transcription in Plasmodium falciparum repeatedly selected for a defined adhesion phenotype. Mol. Microbiol. 56 (2005) 774-788
    • (2005) Mol. Microbiol. , vol.56 , pp. 774-788
    • Duffy, M.F.1
  • 51
    • 0038046769 scopus 로고    scopus 로고
    • Selective upregulation of a single distinctly structured var gene in chondroitin sulphate A-adhering Plasmodium falciparum involved in pregnancy-associated malaria
    • Salanti A., et al. Selective upregulation of a single distinctly structured var gene in chondroitin sulphate A-adhering Plasmodium falciparum involved in pregnancy-associated malaria. Mol. Microbiol. 49 (2003) 179-191
    • (2003) Mol. Microbiol. , vol.49 , pp. 179-191
    • Salanti, A.1
  • 52
    • 14844292560 scopus 로고    scopus 로고
    • Identification of multiple chondroitin sulfate A (CSA)-binding domains in the var2CSA gene transcribed in CSA-binding parasites
    • Gamain B., et al. Identification of multiple chondroitin sulfate A (CSA)-binding domains in the var2CSA gene transcribed in CSA-binding parasites. J. Infect. Dis. 191 (2005) 1010-1013
    • (2005) J. Infect. Dis. , vol.191 , pp. 1010-1013
    • Gamain, B.1
  • 53
    • 35548965232 scopus 로고    scopus 로고
    • VAR2CSA and protective immunity against pregnancy-associated Plasmodium falciparum malaria
    • Hviid L., and Salanti A. VAR2CSA and protective immunity against pregnancy-associated Plasmodium falciparum malaria. Parasitology 134 (2007) 1871-1876
    • (2007) Parasitology , vol.134 , pp. 1871-1876
    • Hviid, L.1    Salanti, A.2
  • 54
    • 0034548046 scopus 로고    scopus 로고
    • Mapping of the region of complement receptor (CR) 1 required for Plasmodium falciparum rosetting and demonstration of the importance of CR1 in rosetting in field isolates
    • Rowe J.A., et al. Mapping of the region of complement receptor (CR) 1 required for Plasmodium falciparum rosetting and demonstration of the importance of CR1 in rosetting in field isolates. J. Immunol. 165 (2000) 6341-6346
    • (2000) J. Immunol. , vol.165 , pp. 6341-6346
    • Rowe, J.A.1
  • 55
    • 0036093067 scopus 로고    scopus 로고
    • Rosetting and autoagglutination in Plasmodium falciparum
    • Fernandez V., and Wahlgren M. Rosetting and autoagglutination in Plasmodium falciparum. Chem. Immunol. 80 (2002) 163-187
    • (2002) Chem. Immunol. , vol.80 , pp. 163-187
    • Fernandez, V.1    Wahlgren, M.2
  • 56
    • 0028260815 scopus 로고
    • Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte
    • Martin S.K., et al. Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte. J. Parasitol. 80 (1994) 371-378
    • (1994) J. Parasitol. , vol.80 , pp. 371-378
    • Martin, S.K.1
  • 57
    • 35648996502 scopus 로고    scopus 로고
    • Plasmodium falciparum ookinetes require mosquito midgut chondroitin sulfate proteoglycans for cell invasion
    • Dinglasan R.R., et al. Plasmodium falciparum ookinetes require mosquito midgut chondroitin sulfate proteoglycans for cell invasion. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 15882-15887
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15882-15887
    • Dinglasan, R.R.1
  • 58
    • 0344420140 scopus 로고    scopus 로고
    • Monoclonal antibody MG96 completely blocks Plasmodium yoelii development in Anopheles stephensi
    • Dinglasan R.R., et al. Monoclonal antibody MG96 completely blocks Plasmodium yoelii development in Anopheles stephensi. Infect. Immun. 71 (2003) 6995-7001
    • (2003) Infect. Immun. , vol.71 , pp. 6995-7001
    • Dinglasan, R.R.1
  • 59
    • 1642301073 scopus 로고    scopus 로고
    • Effects of mosquito genes on Plasmodium development
    • Osta M.A., et al. Effects of mosquito genes on Plasmodium development. Science 303 (2004) 2030-2032
    • (2004) Science , vol.303 , pp. 2030-2032
    • Osta, M.A.1
  • 60
    • 12744268777 scopus 로고    scopus 로고
    • Functional characterization of an LCCL-lectin domain containing protein family in Plasmodium berghei
    • Trueman H.E., et al. Functional characterization of an LCCL-lectin domain containing protein family in Plasmodium berghei. J. Parasitol. 90 (2004) 1062-1071
    • (2004) J. Parasitol. , vol.90 , pp. 1062-1071
    • Trueman, H.E.1
  • 61
    • 0033429047 scopus 로고    scopus 로고
    • Targeted disruption of the Plasmodium berghei CTRP gene reveals its essential role in malaria infection of the vector mosquito
    • Yuda M., et al. Targeted disruption of the Plasmodium berghei CTRP gene reveals its essential role in malaria infection of the vector mosquito. J. Exp. Med. 190 (1999) 1711-1716
    • (1999) J. Exp. Med. , vol.190 , pp. 1711-1716
    • Yuda, M.1
  • 62
    • 0025857170 scopus 로고
    • Malaria parasite chitinase and penetration of the mosquito peritrophic membrane
    • Huber M., et al. Malaria parasite chitinase and penetration of the mosquito peritrophic membrane. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 2807-2810
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2807-2810
    • Huber, M.1
  • 63
    • 0027308860 scopus 로고
    • Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease
    • Shahabuddin M., et al. Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 4266-4270
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 4266-4270
    • Shahabuddin, M.1
  • 64
    • 0035019734 scopus 로고    scopus 로고
    • Knockout of the rodent malaria parasite chitinase pbCHT1 reduces infectivity to mosquitoes
    • Dessens J.T., et al. Knockout of the rodent malaria parasite chitinase pbCHT1 reduces infectivity to mosquitoes. Infect. Immun. 69 (2001) 4041-4047
    • (2001) Infect. Immun. , vol.69 , pp. 4041-4047
    • Dessens, J.T.1
  • 65
    • 0035007319 scopus 로고    scopus 로고
    • Disruption of Plasmodium falciparum chitinase markedly impairs parasite invasion of mosquito midgut
    • Tsai Y.L., et al. Disruption of Plasmodium falciparum chitinase markedly impairs parasite invasion of mosquito midgut. Infect. Immun. 69 (2001) 4048-4054
    • (2001) Infect. Immun. , vol.69 , pp. 4048-4054
    • Tsai, Y.L.1
  • 66
    • 0033598751 scopus 로고    scopus 로고
    • The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences
    • Vinetz J.M., et al. The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 14061-14066
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 14061-14066
    • Vinetz, J.M.1
  • 67
    • 23944443326 scopus 로고    scopus 로고
    • An anti-chitinase malaria transmission-blocking single-chain antibody as an effector molecule for creating a Plasmodium falciparum-refractory mosquito
    • Li F., et al. An anti-chitinase malaria transmission-blocking single-chain antibody as an effector molecule for creating a Plasmodium falciparum-refractory mosquito. J. Infect. Dis. 192 (2005) 878-887
    • (2005) J. Infect. Dis. , vol.192 , pp. 878-887
    • Li, F.1
  • 68
    • 0027471132 scopus 로고
    • Signal transduction in host cells by a glycosylphosphatidylinositol toxin of malaria parasites
    • Schofield L., and Hackett F. Signal transduction in host cells by a glycosylphosphatidylinositol toxin of malaria parasites. J. Exp. Med. 177 (1993) 145-153
    • (1993) J. Exp. Med. , vol.177 , pp. 145-153
    • Schofield, L.1    Hackett, F.2
  • 69
    • 26244442975 scopus 로고    scopus 로고
    • Stimulation of innate immune responses by malarial glycosylphosphatidylinositol via pattern recognition receptors
    • Nebl T., et al. Stimulation of innate immune responses by malarial glycosylphosphatidylinositol via pattern recognition receptors. Parasitology 130 Suppl (2005) S45-S62
    • (2005) Parasitology , vol.130 , Issue.SUPPL
    • Nebl, T.1
  • 70
    • 0037341358 scopus 로고    scopus 로고
    • Regulation of murine cerebral malaria pathogenesis by CD1d-restricted NKT cells and the natural killer complex
    • Hansen D.S., et al. Regulation of murine cerebral malaria pathogenesis by CD1d-restricted NKT cells and the natural killer complex. Immunity 18 (2003) 391-402
    • (2003) Immunity , vol.18 , pp. 391-402
    • Hansen, D.S.1
  • 71
    • 16244370047 scopus 로고    scopus 로고
    • The natural killer complex regulates severe malarial pathogenesis and influences acquired immune responses to Plasmodium berghei ANKA
    • Hansen D.S., et al. The natural killer complex regulates severe malarial pathogenesis and influences acquired immune responses to Plasmodium berghei ANKA. Infect. Immun. 73 (2005) 2288-2297
    • (2005) Infect. Immun. , vol.73 , pp. 2288-2297
    • Hansen, D.S.1
  • 72
    • 25644445145 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositols in malaria pathogenesis and immunity: potential for therapeutic inhibition and vaccination
    • Boutlis C.S., et al. Glycosylphosphatidylinositols in malaria pathogenesis and immunity: potential for therapeutic inhibition and vaccination. Curr. Top. Microbiol. Immunol. 297 (2005) 145-185
    • (2005) Curr. Top. Microbiol. Immunol. , vol.297 , pp. 145-185
    • Boutlis, C.S.1
  • 73
    • 0042866204 scopus 로고    scopus 로고
    • Age-dependent impairment of IgG responses to glycosylphosphatidylinositol with equal exposure to Plasmodium falciparum among Javanese migrants to Papua, Indonesia
    • Hudson Keenihan S.N., et al. Age-dependent impairment of IgG responses to glycosylphosphatidylinositol with equal exposure to Plasmodium falciparum among Javanese migrants to Papua, Indonesia. Am. J. Trop. Med. Hyg. 69 (2003) 36-41
    • (2003) Am. J. Trop. Med. Hyg. , vol.69 , pp. 36-41
    • Hudson Keenihan, S.N.1
  • 74
    • 33749241164 scopus 로고    scopus 로고
    • Fatty acids from Plasmodium falciparum down-regulate the toxic activity of malaria glycosylphosphatidylinositols
    • Debierre-Grockiego F., et al. Fatty acids from Plasmodium falciparum down-regulate the toxic activity of malaria glycosylphosphatidylinositols. Infect. Immun. 74 (2006) 5487-5496
    • (2006) Infect. Immun. , vol.74 , pp. 5487-5496
    • Debierre-Grockiego, F.1


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