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Volumn 40, Issue 10, 2010, Pages 1145-1154

Sialic acids: Key determinants for invasion by the Apicomplexa

Author keywords

Apicomplexa; Glycans; Invasion; Microneme; Plasmodium falciparum; Receptor; Sialic acid; Toxoplasma gondii

Indexed keywords

ERYTHROCYTE ANTIGEN; ERYTHROCYTE MEMBRANE PROTEIN 1; GLYCOPHORIN; SIALIC ACID;

EID: 77954027975     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2010.04.007     Document Type: Review
Times cited : (15)

References (111)
  • 2
    • 77951026559 scopus 로고    scopus 로고
    • Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles
    • Alexander D.L., Mital J., Ward G.E., Bradley P., Boothroyd J.C. Identification of the moving junction complex of Toxoplasma gondii: a collaboration between distinct secretory organelles. PLoS Pathog. 2005, 1:e17.
    • (2005) PLoS Pathog. , vol.1
    • Alexander, D.L.1    Mital, J.2    Ward, G.E.3    Bradley, P.4    Boothroyd, J.C.5
  • 3
    • 34447100360 scopus 로고    scopus 로고
    • Adhesion molecules and other secreted host-interaction determinants in Apicomplexa: insights from comparative genomics
    • Anantharaman V., Iyer L.M., Balaji S., Aravind L. Adhesion molecules and other secreted host-interaction determinants in Apicomplexa: insights from comparative genomics. Int. Rev. Cytol. 2007, 262:1-74.
    • (2007) Int. Rev. Cytol. , vol.262 , pp. 1-74
    • Anantharaman, V.1    Iyer, L.M.2    Balaji, S.3    Aravind, L.4
  • 5
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • Baker R.P., Wijetilaka R., Urban S. Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria. PLoS Pathog. 2006, 2:e113.
    • (2006) PLoS Pathog. , vol.2
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 6
    • 15944368914 scopus 로고    scopus 로고
    • Transepithelial migration of Toxoplasma gondii involves an interaction of intercellular adhesion molecule 1 (ICAM-1) with the parasite adhesin MIC2
    • Barragan A., Brossier F., Sibley L.D. Transepithelial migration of Toxoplasma gondii involves an interaction of intercellular adhesion molecule 1 (ICAM-1) with the parasite adhesin MIC2. Cell. Microbiol. 2005, 7:561-568.
    • (2005) Cell. Microbiol. , vol.7 , pp. 561-568
    • Barragan, A.1    Brossier, F.2    Sibley, L.D.3
  • 7
    • 0344405679 scopus 로고    scopus 로고
    • Erythrocyte invasion phenotypes of Plasmodium falciparum in The Gambia
    • Baum J., Pinder M., Conway D.J. Erythrocyte invasion phenotypes of Plasmodium falciparum in The Gambia. Infect. Immun. 2003, 71:1856-1863.
    • (2003) Infect. Immun. , vol.71 , pp. 1856-1863
    • Baum, J.1    Pinder, M.2    Conway, D.J.3
  • 9
    • 34047147102 scopus 로고    scopus 로고
    • Variant merozoite protein expression is associated with erythrocyte invasion phenotypes in Plasmodium falciparum isolates from Tanzania
    • Bei A.K., Membi C.D., Rayner J.C., Mubi M., Ngasala B., Sultan A.A., Premji Z., Duraisingh M.T. Variant merozoite protein expression is associated with erythrocyte invasion phenotypes in Plasmodium falciparum isolates from Tanzania. Mol. Biochem. Parasitol. 2007, 153:66-71.
    • (2007) Mol. Biochem. Parasitol. , vol.153 , pp. 66-71
    • Bei, A.K.1    Membi, C.D.2    Rayner, J.C.3    Mubi, M.4    Ngasala, B.5    Sultan, A.A.6    Premji, Z.7    Duraisingh, M.T.8
  • 12
    • 0037458587 scopus 로고    scopus 로고
    • C-terminal processing of the Toxoplasma protein MIC2 is essential for invasion into host cells
    • Brossier F., Jewett T.J., Lovett J.L., Sibley L.D. C-terminal processing of the Toxoplasma protein MIC2 is essential for invasion into host cells. J. Biol. Chem. 2003, 278:6229-6234.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6229-6234
    • Brossier, F.1    Jewett, T.J.2    Lovett, J.L.3    Sibley, L.D.4
  • 13
    • 15244360655 scopus 로고    scopus 로고
    • A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma
    • Brossier F., Jewett T.J., Sibley L.D., Urban S. A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Proc. Natl. Acad. Sci. USA 2005, 102:4146-4151.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4146-4151
    • Brossier, F.1    Jewett, T.J.2    Sibley, L.D.3    Urban, S.4
  • 14
    • 0034654252 scopus 로고    scopus 로고
    • A microneme protein from Eimeria tenella with homology to the Apple domains of coagulation factor XI and plasma pre-kallikrein
    • Brown P.J., Billington K.J., Bumstead J.M., Clark J.D., Tomley F.M. A microneme protein from Eimeria tenella with homology to the Apple domains of coagulation factor XI and plasma pre-kallikrein. Mol. Biochem. Parasitol. 2000, 107:91-102.
    • (2000) Mol. Biochem. Parasitol. , vol.107 , pp. 91-102
    • Brown, P.J.1    Billington, K.J.2    Bumstead, J.M.3    Clark, J.D.4    Tomley, F.M.5
  • 15
    • 33846860640 scopus 로고    scopus 로고
    • Pulling together: an integrated model of Toxoplasma cell invasion
    • Carruthers V., Boothroyd J.C. Pulling together: an integrated model of Toxoplasma cell invasion. Curr. Opin. Microbiol. 2007, 10:83-89.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 83-89
    • Carruthers, V.1    Boothroyd, J.C.2
  • 16
    • 0030956863 scopus 로고    scopus 로고
    • Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts
    • Carruthers V.B., Sibley L.D. Sequential protein secretion from three distinct organelles of Toxoplasma gondii accompanies invasion of human fibroblasts. Eur. J. Cell Biol. 1997, 73:114-123.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 114-123
    • Carruthers, V.B.1    Sibley, L.D.2
  • 17
    • 0033224351 scopus 로고    scopus 로고
    • Secretion of micronemal proteins is associated with Toxoplasma invasion of host cells
    • Carruthers V.B., Giddings O.K., Sibley L.D. Secretion of micronemal proteins is associated with Toxoplasma invasion of host cells. Cell. Microbiol. 1999, 1:225-235.
    • (1999) Cell. Microbiol. , vol.1 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 18
    • 0034640516 scopus 로고    scopus 로고
    • The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases
    • Carruthers V.B., Sherman G.D., Sibley L.D. The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases. J. Biol. Chem. 2000, 275:14346-14353.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14346-14353
    • Carruthers, V.B.1    Sherman, G.D.2    Sibley, L.D.3
  • 20
    • 0026795458 scopus 로고
    • The basolateral domain of the hepatocyte plasma membrane bears receptors for the circumsporozoite protein of Plasmodium falciparum sporozoites
    • Cerami C., Frevert U., Sinnis P., Takacs B., Clavijo P., Santos M.J., Nussenzweig V. The basolateral domain of the hepatocyte plasma membrane bears receptors for the circumsporozoite protein of Plasmodium falciparum sporozoites. Cell 1992, 70:1021-1033.
    • (1992) Cell , vol.70 , pp. 1021-1033
    • Cerami, C.1    Frevert, U.2    Sinnis, P.3    Takacs, B.4    Clavijo, P.5    Santos, M.J.6    Nussenzweig, V.7
  • 21
    • 0037013918 scopus 로고    scopus 로고
    • The Toxoplasma gondii protein MIC3 requires pro-peptide cleavage and dimerization to function as adhesin
    • Cerede O., Dubremetz J.F., Bout D., Lebrun M. The Toxoplasma gondii protein MIC3 requires pro-peptide cleavage and dimerization to function as adhesin. EMBO J. 2002, 21:2526-2536.
    • (2002) EMBO J. , vol.21 , pp. 2526-2536
    • Cerede, O.1    Dubremetz, J.F.2    Bout, D.3    Lebrun, M.4
  • 23
    • 56349152375 scopus 로고    scopus 로고
    • In silico identification of specialized secretory-organelle proteins in apicomplexan parasites and in vivo validation in Toxoplasma gondii
    • Chen Z., Harb O.S., Roos D.S. In silico identification of specialized secretory-organelle proteins in apicomplexan parasites and in vivo validation in Toxoplasma gondii. PLoS One 2008, 3:e3611.
    • (2008) PLoS One , vol.3
    • Chen, Z.1    Harb, O.S.2    Roos, D.S.3
  • 25
    • 48849109895 scopus 로고    scopus 로고
    • The terminal sialic acid of glycoconjugates on the surface of intestinal epithelial cells activates excystation of Cryptosporidium parvum
    • Choudhry N., Bajaj-Elliott M., McDonald V. The terminal sialic acid of glycoconjugates on the surface of intestinal epithelial cells activates excystation of Cryptosporidium parvum. Infect. Immun. 2008, 76:3735-3741.
    • (2008) Infect. Immun. , vol.76 , pp. 3735-3741
    • Choudhry, N.1    Bajaj-Elliott, M.2    McDonald, V.3
  • 26
    • 70449489535 scopus 로고    scopus 로고
    • ABO blood group glycans modulate sialic acid recognition on erythrocytes
    • Cohen M., Hurtado-Ziola N., Varki A. ABO blood group glycans modulate sialic acid recognition on erythrocytes. Blood 2009, 114:3668-3676.
    • (2009) Blood , vol.114 , pp. 3668-3676
    • Cohen, M.1    Hurtado-Ziola, N.2    Varki, A.3
  • 29
    • 4143127652 scopus 로고    scopus 로고
    • Host cell invasion by the apicomplexans: the significance of microneme protein proteolysis
    • Dowse T., Soldati D. Host cell invasion by the apicomplexans: the significance of microneme protein proteolysis. Curr. Opin. Microbiol. 2004, 7:388-396.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 388-396
    • Dowse, T.1    Soldati, D.2
  • 30
    • 19444382777 scopus 로고    scopus 로고
    • Apicomplexan rhomboids have a potential role in microneme protein cleavage during host cell invasion
    • Dowse T.J., Pascall J.C., Brown K.D., Soldati D. Apicomplexan rhomboids have a potential role in microneme protein cleavage during host cell invasion. Int. J. Parasitol. 2005, 35:747-756.
    • (2005) Int. J. Parasitol. , vol.35 , pp. 747-756
    • Dowse, T.J.1    Pascall, J.C.2    Brown, K.D.3    Soldati, D.4
  • 31
    • 0037447273 scopus 로고    scopus 로고
    • Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways
    • Duraisingh M.T., Maier A.G., Triglia T., Cowman A.F. Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways. Proc. Natl. Acad. Sci. USA 2003, 100:4796-4801.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4796-4801
    • Duraisingh, M.T.1    Maier, A.G.2    Triglia, T.3    Cowman, A.F.4
  • 32
    • 0037416197 scopus 로고    scopus 로고
    • Phenotypic variation of Plasmodium falciparum merozoite proteins directs receptor targeting for invasion of human erythrocytes
    • Duraisingh M.T., Triglia T., Ralph S.A., Rayner J.C., Barnwell J.W., McFadden G.I., Cowman A.F. Phenotypic variation of Plasmodium falciparum merozoite proteins directs receptor targeting for invasion of human erythrocytes. EMBO J. 2003, 22:1047-1057.
    • (2003) EMBO J. , vol.22 , pp. 1047-1057
    • Duraisingh, M.T.1    Triglia, T.2    Ralph, S.A.3    Rayner, J.C.4    Barnwell, J.W.5    McFadden, G.I.6    Cowman, A.F.7
  • 34
    • 0027090147 scopus 로고
    • Microneme secretion in Coccidia: confocal laser scanning and electron microscope study of Sarcocystis muris in cell culture
    • Entzeroth R., Kerckhoff H., Konig A. Microneme secretion in Coccidia: confocal laser scanning and electron microscope study of Sarcocystis muris in cell culture. Eur. J. Cell Biol. 1992, 59:405-413.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 405-413
    • Entzeroth, R.1    Kerckhoff, H.2    Konig, A.3
  • 36
    • 0344874620 scopus 로고    scopus 로고
    • Determination of the genera of cyst-forming coccidia
    • Frenkel J.K., Smith D.D. Determination of the genera of cyst-forming coccidia. Parasitol. Res. 2003, 91:384-389.
    • (2003) Parasitol. Res. , vol.91 , pp. 384-389
    • Frenkel, J.K.1    Smith, D.D.2
  • 37
    • 76249095009 scopus 로고    scopus 로고
    • Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites
    • Friedrich N., Santos J.M., Liu Y., Palma A.S., Leon E., Saouros S., Kiso M., Blackman M.J., Matthews S., Feizi T., Soldati-Favre D. Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites. J. Biol. Chem. 2010, 285:2064-2076.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2064-2076
    • Friedrich, N.1    Santos, J.M.2    Liu, Y.3    Palma, A.S.4    Leon, E.5    Saouros, S.6    Kiso, M.7    Blackman, M.J.8    Matthews, S.9    Feizi, T.10    Soldati-Favre, D.11
  • 38
    • 0022256777 scopus 로고
    • Embryonal lactosaminoglycan. The structure of branched lactosaminoglycans with novel disialosyl (sialyl alpha 2-9 sialyl) terminals isolated from PA1 human embryonal carcinoma cells
    • Fukuda M.N., Dell A., Oates J.E., Fukuda M. Embryonal lactosaminoglycan. The structure of branched lactosaminoglycans with novel disialosyl (sialyl alpha 2-9 sialyl) terminals isolated from PA1 human embryonal carcinoma cells. J. Biol. Chem. 1985, 260:6623-6631.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6623-6631
    • Fukuda, M.N.1    Dell, A.2    Oates, J.E.3    Fukuda, M.4
  • 39
    • 0242636104 scopus 로고    scopus 로고
    • Babesia bovis merozoites invade human, ovine, equine, porcine and caprine erythrocytes by a sialic acid-dependent mechanism followed by developmental arrest after a single round of cell fission
    • Gaffar F.R., Franssen F.F., de Vries E. Babesia bovis merozoites invade human, ovine, equine, porcine and caprine erythrocytes by a sialic acid-dependent mechanism followed by developmental arrest after a single round of cell fission. Int. J. Parasitol. 2003, 33:1595-1603.
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1595-1603
    • Gaffar, F.R.1    Franssen, F.F.2    de Vries, E.3
  • 40
    • 0026716618 scopus 로고
    • A reticulocyte-binding protein complex of Plasmodium vivax merozoites
    • Galinski M.R., Medina C.C., Ingravallo P., Barnwell J.W. A reticulocyte-binding protein complex of Plasmodium vivax merozoites. Cell 1992, 69:1213-1226.
    • (1992) Cell , vol.69 , pp. 1213-1226
    • Galinski, M.R.1    Medina, C.C.2    Ingravallo, P.3    Barnwell, J.W.4
  • 43
    • 36749018054 scopus 로고    scopus 로고
    • Recombinant Plasmodium falciparum reticulocyte homology protein 4 binds to erythrocytes and blocks invasion
    • Gaur D., Singh S., Jiang L., Diouf A., Miller L.H. Recombinant Plasmodium falciparum reticulocyte homology protein 4 binds to erythrocytes and blocks invasion. Proc. Natl. Acad. Sci USA 2007, 104:17789-17794.
    • (2007) Proc. Natl. Acad. Sci USA , vol.104 , pp. 17789-17794
    • Gaur, D.1    Singh, S.2    Jiang, L.3    Diouf, A.4    Miller, L.H.5
  • 44
    • 0042672913 scopus 로고    scopus 로고
    • The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking
    • Gilberger T.W., Thompson J.K., Reed M.B., Good R.T., Cowman A.F. The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking. J. Cell Biol. 2003, 162:317-327.
    • (2003) J. Cell Biol. , vol.162 , pp. 317-327
    • Gilberger, T.W.1    Thompson, J.K.2    Reed, M.B.3    Good, R.T.4    Cowman, A.F.5
  • 45
    • 0023567278 scopus 로고
    • Falciparum malaria parasites invade erythrocytes that lack glycophorin A and B (MkMk). Strain differences indicate receptor heterogeneity and two pathways for invasion
    • Hadley T.J., Klotz F.W., Pasvol G., Haynes J.D., McGinniss M.H., Okubo Y., Miller L.H. Falciparum malaria parasites invade erythrocytes that lack glycophorin A and B (MkMk). Strain differences indicate receptor heterogeneity and two pathways for invasion. J. Clin. Invest. 1987, 80:1190-1193.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1190-1193
    • Hadley, T.J.1    Klotz, F.W.2    Pasvol, G.3    Haynes, J.D.4    McGinniss, M.H.5    Okubo, Y.6    Miller, L.H.7
  • 46
    • 1542375192 scopus 로고    scopus 로고
    • Multimerization of the Toxoplasma gondii MIC2 integrin-like A-domain is required for binding to heparin and human cells
    • Harper J.M., Hoff E.F., Carruthers V.B. Multimerization of the Toxoplasma gondii MIC2 integrin-like A-domain is required for binding to heparin and human cells. Mol. Biochem. Parasitol. 2004, 134:201-212.
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 201-212
    • Harper, J.M.1    Hoff, E.F.2    Carruthers, V.B.3
  • 47
    • 33749484972 scopus 로고    scopus 로고
    • A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex
    • Harper J.M., Huynh M.H., Coppens I., Parussini F., Moreno S., Carruthers V.B. A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex. Mol. Biol. Cell 2006, 17:4551-4563.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4551-4563
    • Harper, J.M.1    Huynh, M.H.2    Coppens, I.3    Parussini, F.4    Moreno, S.5    Carruthers, V.B.6
  • 49
    • 0038267453 scopus 로고    scopus 로고
    • A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage
    • Howell S.A., Well I., Fleck S.L., Kettleborough C., Collins C.R., Blackman M.J. A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage. J. Biol. Chem. 2003, 278:23890-23898.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23890-23898
    • Howell, S.A.1    Well, I.2    Fleck, S.L.3    Kettleborough, C.4    Collins, C.R.5    Blackman, M.J.6
  • 51
    • 0042027767 scopus 로고    scopus 로고
    • Ultrasensitive analysis of sialic acids and oligo/polysialic acids by fluorometric high-performance liquid chromatography
    • Inoue S., Inoue Y. Ultrasensitive analysis of sialic acids and oligo/polysialic acids by fluorometric high-performance liquid chromatography. Methods Enzymol. 2003, 362:543-560.
    • (2003) Methods Enzymol. , vol.362 , pp. 543-560
    • Inoue, S.1    Inoue, Y.2
  • 52
    • 0041854147 scopus 로고    scopus 로고
    • Solubilisation and properties of the sialate-4-O-acetyltransferase from guinea pig liver
    • Iwersen M., Dora H., Kohla G., Gasa S., Schauer R. Solubilisation and properties of the sialate-4-O-acetyltransferase from guinea pig liver. Biol. Chem. 2003, 384:1035-1047.
    • (2003) Biol. Chem. , vol.384 , pp. 1035-1047
    • Iwersen, M.1    Dora, H.2    Kohla, G.3    Gasa, S.4    Schauer, R.5
  • 54
    • 3342944910 scopus 로고    scopus 로고
    • Identification and characterization of a Neospora caninum microneme-associated protein (NcMIC4) that exhibits unique lactose-binding properties
    • Keller N., Riesen M., Naguleswaran A., Vonlaufen N., Stettler R., Leepin A., Wastling J.M., Hemphill A. Identification and characterization of a Neospora caninum microneme-associated protein (NcMIC4) that exhibits unique lactose-binding properties. Infect. Immun. 2004, 72:4791-4800.
    • (2004) Infect. Immun. , vol.72 , pp. 4791-4800
    • Keller, N.1    Riesen, M.2    Naguleswaran, A.3    Vonlaufen, N.4    Stettler, R.5    Leepin, A.6    Wastling, J.M.7    Hemphill, A.8
  • 56
    • 0031809626 scopus 로고    scopus 로고
    • Expression, purification, and biochemical characterization of a recombinant lectin of Sarcocystis muris (Apicomplexa) cyst merozoites
    • Klein H., Loschner B., Zyto N., Portner M., Montag T. Expression, purification, and biochemical characterization of a recombinant lectin of Sarcocystis muris (Apicomplexa) cyst merozoites. Glycoconj. J. 1998, 15:147-153.
    • (1998) Glycoconj. J. , vol.15 , pp. 147-153
    • Klein, H.1    Loschner, B.2    Zyto, N.3    Portner, M.4    Montag, T.5
  • 57
    • 0037616551 scopus 로고    scopus 로고
    • Cloning, sequencing and recombinant expression of the open reading frame encoding a novel member of the Sarcocystis muris (Apicomplexa) microneme lectin family
    • Klein H., Mueller S., Loeschner B., Toenjes R.R., Braun G., Mueller E.C., Otto A., Montag T. Cloning, sequencing and recombinant expression of the open reading frame encoding a novel member of the Sarcocystis muris (Apicomplexa) microneme lectin family. Parasitol. Res. 2003, 90:84-86.
    • (2003) Parasitol. Res. , vol.90 , pp. 84-86
    • Klein, H.1    Mueller, S.2    Loeschner, B.3    Toenjes, R.R.4    Braun, G.5    Mueller, E.C.6    Otto, A.7    Montag, T.8
  • 58
    • 33845438029 scopus 로고    scopus 로고
    • Endogenous development, pathogenicity and host specificity of Eimeria cahirinensis Couch, Blaustein, Duszynski, Shenbrot and Nevo, 1997 (Apicomplexa: Eimeriidae) from Acomys dimidiatus (Cretzschmar 1826) (Rodentia: Muridae) from the Near East
    • Kvicerova J., Ptackova P., Modry D. Endogenous development, pathogenicity and host specificity of Eimeria cahirinensis Couch, Blaustein, Duszynski, Shenbrot and Nevo, 1997 (Apicomplexa: Eimeriidae) from Acomys dimidiatus (Cretzschmar 1826) (Rodentia: Muridae) from the Near East. Parasitol. Res. 2007, 100:219-226.
    • (2007) Parasitol. Res. , vol.100 , pp. 219-226
    • Kvicerova, J.1    Ptackova, P.2    Modry, D.3
  • 60
    • 70350417600 scopus 로고    scopus 로고
    • Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl
    • Larson E.T., Parussini F., Huynh M.H., Giebel J.D., Kelley A.M., Zhang L., Bogyo M., Merritt E.A., Carruthers V.B. Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl. J. Biol. Chem. 2009, 284:26839-26850.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26839-26850
    • Larson, E.T.1    Parussini, F.2    Huynh, M.H.3    Giebel, J.D.4    Kelley, A.M.5    Zhang, L.6    Bogyo, M.7    Merritt, E.A.8    Carruthers, V.B.9
  • 61
    • 0024065390 scopus 로고
    • Cross-transmission of Eimeria spp. (Protozoa, Apicomplexa) of rodents - a review
    • Levine N.D., Ivens V. Cross-transmission of Eimeria spp. (Protozoa, Apicomplexa) of rodents - a review. J. Protozool. 1988, 35:434-437.
    • (1988) J. Protozool. , vol.35 , pp. 434-437
    • Levine, N.D.1    Ivens, V.2
  • 62
    • 0037234392 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations
    • Maier A.G., Duraisingh M.T., Reeder J.C., Patel S.S., Kazura J.W., Zimmerman P.A., Cowman A.F. Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations. Nat. Med. 2003, 9:87-92.
    • (2003) Nat. Med. , vol.9 , pp. 87-92
    • Maier, A.G.1    Duraisingh, M.T.2    Reeder, J.C.3    Patel, S.S.4    Kazura, J.W.5    Zimmerman, P.A.6    Cowman, A.F.7
  • 63
    • 63149115957 scopus 로고    scopus 로고
    • Polymorphisms in erythrocyte binding antigens 140 and 181 affect function and binding but not receptor specificity in Plasmodium falciparum
    • Maier A.G., Baum J., Smith B., Conway D.J., Cowman A.F. Polymorphisms in erythrocyte binding antigens 140 and 181 affect function and binding but not receptor specificity in Plasmodium falciparum. Infect. Immun. 2009, 77:1689-1699.
    • (2009) Infect. Immun. , vol.77 , pp. 1689-1699
    • Maier, A.G.1    Baum, J.2    Smith, B.3    Conway, D.J.4    Cowman, A.F.5
  • 64
    • 24644481321 scopus 로고    scopus 로고
    • Evolution of human-chimpanzee differences in malaria susceptibility: relationship to human genetic loss of N-glycolylneuraminic acid
    • Martin M.J., Rayner J.C., Gagneux P., Barnwell J.W., Varki A. Evolution of human-chimpanzee differences in malaria susceptibility: relationship to human genetic loss of N-glycolylneuraminic acid. Proc. Natl. Acad. Sci. USA 2005, 102:12819-12824.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12819-12824
    • Martin, M.J.1    Rayner, J.C.2    Gagneux, P.3    Barnwell, J.W.4    Varki, A.5
  • 65
    • 33144460574 scopus 로고    scopus 로고
    • The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL
    • Mayer D.C., Jiang L., Achur R.N., Kakizaki I., Gowda D.C., Miller L.H. The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL. Proc. Natl. Acad. Sci. USA 2006, 103:2358-2362.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2358-2362
    • Mayer, D.C.1    Jiang, L.2    Achur, R.N.3    Kakizaki, I.4    Gowda, D.C.5    Miller, L.H.6
  • 68
    • 0016592489 scopus 로고
    • Erythrocyte receptors for (Plasmodium knowlesi) malaria: Duffy blood group determinants
    • Miller L.H., Mason S.J., Dvorak J.A., McGinniss M.H., Rothman I.K. Erythrocyte receptors for (Plasmodium knowlesi) malaria: Duffy blood group determinants. Science 1975, 189:561-563.
    • (1975) Science , vol.189 , pp. 561-563
    • Miller, L.H.1    Mason, S.J.2    Dvorak, J.A.3    McGinniss, M.H.4    Rothman, I.K.5
  • 69
    • 0017077503 scopus 로고
    • The resistance factor to Plasmodium vivax in blacks. The Duffy-blood-group genotype, FyFy
    • Miller L.H., Mason S.J., Clyde D.F., McGinniss M.H. The resistance factor to Plasmodium vivax in blacks. The Duffy-blood-group genotype, FyFy. N. Engl. J. Med. 1976, 295:302-304.
    • (1976) N. Engl. J. Med. , vol.295 , pp. 302-304
    • Miller, L.H.1    Mason, S.J.2    Clyde, D.F.3    McGinniss, M.H.4
  • 70
    • 0017388354 scopus 로고
    • Evidence for differences in erythrocyte surface receptors for the malarial parasites, Plasmodium falciparum and Plasmodium knowlesi
    • Miller L.H., Haynes J.D., McAuliffe F.M., Shiroishi T., Durocher J.R., McGinniss M.H. Evidence for differences in erythrocyte surface receptors for the malarial parasites, Plasmodium falciparum and Plasmodium knowlesi. J. Exp. Med. 1977, 146:277-281.
    • (1977) J. Exp. Med. , vol.146 , pp. 277-281
    • Miller, L.H.1    Haynes, J.D.2    McAuliffe, F.M.3    Shiroishi, T.4    Durocher, J.R.5    McGinniss, M.H.6
  • 71
    • 0032528078 scopus 로고    scopus 로고
    • Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells
    • Monteiro V.G., Soares C.P., de Souza W. Host cell surface sialic acid residues are involved on the process of penetration of Toxoplasma gondii into mammalian cells. FEMS Microbiol. Lett. 1998, 164:323-327.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 323-327
    • Monteiro, V.G.1    Soares, C.P.2    de Souza, W.3
  • 72
    • 0032755651 scopus 로고    scopus 로고
    • Plasmodium falciparum field isolates commonly use erythrocyte invasion pathways that are independent of sialic acid residues of glycophorin A
    • Okoyeh J.N., Pillai C.R., Chitnis C.E. Plasmodium falciparum field isolates commonly use erythrocyte invasion pathways that are independent of sialic acid residues of glycophorin A. Infect. Immun. 1999, 67:5784-5791.
    • (1999) Infect. Immun. , vol.67 , pp. 5784-5791
    • Okoyeh, J.N.1    Pillai, C.R.2    Chitnis, C.E.3
  • 73
    • 0037007235 scopus 로고    scopus 로고
    • Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii
    • Opitz C., Di Cristina M., Reiss M., Ruppert T., Crisanti A., Soldati D. Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii. EMBO J. 2002, 21:1577-1585.
    • (2002) EMBO J. , vol.21 , pp. 1577-1585
    • Opitz, C.1    Di Cristina, M.2    Reiss, M.3    Ruppert, T.4    Crisanti, A.5    Soldati, D.6
  • 74
    • 0026601423 scopus 로고
    • A malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(alpha 2-3)Gal-sequences of glycophorin A
    • Orlandi P.A., Klotz F.W., Haynes J.D. A malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(alpha 2-3)Gal-sequences of glycophorin A. J. Cell Biol. 1992, 116:901-909.
    • (1992) J. Cell Biol. , vol.116 , pp. 901-909
    • Orlandi, P.A.1    Klotz, F.W.2    Haynes, J.D.3
  • 75
    • 0020687599 scopus 로고
    • Glycophorins and red cell invasion by Plasmodium falciparum
    • Pasvol G., Jungery M. Glycophorins and red cell invasion by Plasmodium falciparum. Ciba Found. Symp. 1983, 94:174-195.
    • (1983) Ciba Found. Symp. , vol.94 , pp. 174-195
    • Pasvol, G.1    Jungery, M.2
  • 76
    • 34447114485 scopus 로고    scopus 로고
    • The microneme proteins EtMIC4 and EtMIC5 of Eimeria tenella form a novel, ultra-high molecular mass protein complex that binds target host cells
    • Periz J., Gill A.C., Hunt L., Brown P., Tomley F.M. The microneme proteins EtMIC4 and EtMIC5 of Eimeria tenella form a novel, ultra-high molecular mass protein complex that binds target host cells. J. Biol. Chem. 2007, 282:16891-16898.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16891-16898
    • Periz, J.1    Gill, A.C.2    Hunt, L.3    Brown, P.4    Tomley, F.M.5
  • 77
    • 0023640268 scopus 로고
    • Erythrocyte receptor recognition varies in Plasmodium falciparum isolates
    • Perkins M.E., Holt E.H. Erythrocyte receptor recognition varies in Plasmodium falciparum isolates. Mol. Biochem. Parasitol 1988, 27:23-34.
    • (1988) Mol. Biochem. Parasitol , vol.27 , pp. 23-34
    • Perkins, M.E.1    Holt, E.H.2
  • 78
  • 80
    • 0035803370 scopus 로고    scopus 로고
    • A Plasmodium falciparum homologue of Plasmodium vivax reticulocyte binding protein (PvRBP1) defines a trypsin-resistant erythrocyte invasion pathway
    • Rayner J.C., Vargas-Serrato E., Huber C.S., Galinski M.R., Barnwell J.W. A Plasmodium falciparum homologue of Plasmodium vivax reticulocyte binding protein (PvRBP1) defines a trypsin-resistant erythrocyte invasion pathway. J. Exp. Med. 2001, 194:1571-1581.
    • (2001) J. Exp. Med. , vol.194 , pp. 1571-1581
    • Rayner, J.C.1    Vargas-Serrato, E.2    Huber, C.S.3    Galinski, M.R.4    Barnwell, J.W.5
  • 81
    • 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., Caruana S.R., Batchelor A.H., Thompson J.K., Crabb B.S., Cowman A.F. 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. USA 2000, 97:7509-7514.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7509-7514
    • Reed, M.B.1    Caruana, S.R.2    Batchelor, A.H.3    Thompson, J.K.4    Crabb, B.S.5    Cowman, A.F.6
  • 84
    • 77952007992 scopus 로고    scopus 로고
    • Interaction between Plasmodium falciparum apical membrane antigen 1 and the Rhoptry neck protein complex defines a key step in the erythrocyte invasion process of malaria parasites
    • Richard D., Macraild C.A., Riglar D.T., Chan J.A., Foley M., Baum J., Ralph S.A., Norton R.S., Cowman A.F. Interaction between Plasmodium falciparum apical membrane antigen 1 and the Rhoptry neck protein complex defines a key step in the erythrocyte invasion process of malaria parasites. J. Biol. Chem. 2010, 285:14815-14822.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14815-14822
    • Richard, D.1    Macraild, C.A.2    Riglar, D.T.3    Chan, J.A.4    Foley, M.5    Baum, J.6    Ralph, S.A.7    Norton, R.S.8    Cowman, A.F.9
  • 85
    • 33645457151 scopus 로고    scopus 로고
    • Localisation and distribution of O-acetylated N-acetylneuraminic acids, the endogenous substrates of the hemagglutinin-esterases of murine coronaviruses, in mouse tissue
    • Rinninger A., Richet C., Pons A., Kohla G., Schauer R., Bauer H.C., Zanetta J.P., Vlasak R. Localisation and distribution of O-acetylated N-acetylneuraminic acids, the endogenous substrates of the hemagglutinin-esterases of murine coronaviruses, in mouse tissue. Glycoconj. J. 2006, 23:73-84.
    • (2006) Glycoconj. J. , vol.23 , pp. 73-84
    • Rinninger, A.1    Richet, C.2    Pons, A.3    Kohla, G.4    Schauer, R.5    Bauer, H.C.6    Zanetta, J.P.7    Vlasak, R.8
  • 90
    • 77649263117 scopus 로고    scopus 로고
    • Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites
    • Singh S., Alam M.M., Pal-Bhowmick I., Brzostowski J.A., Chitnis C.E. Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites. PLoS Pathog. 2010, 6:e1000746.
    • (2010) PLoS Pathog. , vol.6
    • Singh, S.1    Alam, M.M.2    Pal-Bhowmick, I.3    Brzostowski, J.A.4    Chitnis, C.E.5
  • 91
    • 32544440337 scopus 로고    scopus 로고
    • Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain
    • Singh S.K., Hora R., Belrhali H., Chitnis C.E., Sharma A. Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain. Nature 2006, 439:741-744.
    • (2006) Nature , vol.439 , pp. 741-744
    • Singh, S.K.1    Hora, R.2    Belrhali, H.3    Chitnis, C.E.4    Sharma, A.5
  • 92
    • 51149102047 scopus 로고    scopus 로고
    • Molecular dissection of host cell invasion by the apicomplexans: the glideosome
    • Soldati-Favre D. Molecular dissection of host cell invasion by the apicomplexans: the glideosome. Parasite 2008, 15:197-205.
    • (2008) Parasite , vol.15 , pp. 197-205
    • Soldati-Favre, D.1
  • 96
    • 58149460679 scopus 로고    scopus 로고
    • Isolation and pathogenic characterization of an OB1 variant of Babesia rodhaini which has a glycophorin A-independent pathway to murine red blood cells
    • Takabatake N., Iseki H., Ikehara Y., Kanuka H., Yokoyama N., Sekimizu K., Igarashi I. Isolation and pathogenic characterization of an OB1 variant of Babesia rodhaini which has a glycophorin A-independent pathway to murine red blood cells. Vet. Parasitol. 2009, 159:97-104.
    • (2009) Vet. Parasitol. , vol.159 , pp. 97-104
    • Takabatake, N.1    Iseki, H.2    Ikehara, Y.3    Kanuka, H.4    Yokoyama, N.5    Sekimizu, K.6    Igarashi, I.7
  • 97
    • 34247241668 scopus 로고    scopus 로고
    • Whole-genome natural histories of apicomplexan surface proteins
    • Templeton T.J. Whole-genome natural histories of apicomplexan surface proteins. Trends. Parasitol. 2007, 23:205-212.
    • (2007) Trends. Parasitol. , vol.23 , pp. 205-212
    • Templeton, T.J.1
  • 98
    • 0034939850 scopus 로고    scopus 로고
    • A novel ligand from Plasmodium falciparum that binds to a sialic acid-containing receptor on the surface of human erythrocytes
    • Thompson J.K., Triglia T., Reed M.B., Cowman A.F. A novel ligand from Plasmodium falciparum that binds to a sialic acid-containing receptor on the surface of human erythrocytes. Mol. Microbiol. 2001, 41:47-58.
    • (2001) Mol. Microbiol. , vol.41 , pp. 47-58
    • Thompson, J.K.1    Triglia, T.2    Reed, M.B.3    Cowman, A.F.4
  • 99
    • 0035019694 scopus 로고    scopus 로고
    • Mix and match modules: structure and function of microneme proteins in apicomplexan parasites
    • Tomley F.M., Soldati D.S. Mix and match modules: structure and function of microneme proteins in apicomplexan parasites. Trends Para 2001, 17:81-88.
    • (2001) Trends Para , vol.17 , pp. 81-88
    • Tomley, F.M.1    Soldati, D.S.2
  • 100
    • 22744456158 scopus 로고    scopus 로고
    • Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum
    • Tolia N.H., Enemark E.J., Sim B.K., Joshua-Tor L. Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum. Cell 2005, 122:183-193.
    • (2005) Cell , vol.122 , pp. 183-193
    • Tolia, N.H.1    Enemark, E.J.2    Sim, B.K.3    Joshua-Tor, L.4
  • 101
    • 33845974900 scopus 로고    scopus 로고
    • A conserved region in the EBL proteins is implicated in microneme targeting of the malaria parasite Plasmodium falciparum
    • Treeck M., Struck N.S., Haase S., Langer C., Herrmann S., Healer J., Cowman A.F., Gilberger T.W. A conserved region in the EBL proteins is implicated in microneme targeting of the malaria parasite Plasmodium falciparum. J. Biol. Chem. 2006, 281:31995-32003.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31995-32003
    • Treeck, M.1    Struck, N.S.2    Haase, S.3    Langer, C.4    Herrmann, S.5    Healer, J.6    Cowman, A.F.7    Gilberger, T.W.8
  • 103
    • 0035140139 scopus 로고    scopus 로고
    • Identification of proteins from Plasmodium falciparum that are homologous to reticulocyte binding proteins in Plasmodium vivax
    • Triglia T., Thompson J., Caruana S.R., Delorenzi M., Speed T., Cowman A.F. Identification of proteins from Plasmodium falciparum that are homologous to reticulocyte binding proteins in Plasmodium vivax. Infect. Immun. 2001, 69:1084-1092.
    • (2001) Infect. Immun. , vol.69 , pp. 1084-1092
    • Triglia, T.1    Thompson, J.2    Caruana, S.R.3    Delorenzi, M.4    Speed, T.5    Cowman, A.F.6
  • 104
    • 12344304667 scopus 로고    scopus 로고
    • Reticulocyte-binding protein homologue 1 is required for sialic acid-dependent invasion into human erythrocytes by Plasmodium falciparum
    • Triglia T., Duraisingh M.T., Good R.T., Cowman A.F. Reticulocyte-binding protein homologue 1 is required for sialic acid-dependent invasion into human erythrocytes by Plasmodium falciparum. Mol. Microbiol. 2005, 55:162-174.
    • (2005) Mol. Microbiol. , vol.55 , pp. 162-174
    • Triglia, T.1    Duraisingh, M.T.2    Good, R.T.3    Cowman, A.F.4
  • 105
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki A. Sialic acids as ligands in recognition phenomena. FASEB J. 1997, 11:248-255.
    • (1997) FASEB J. , vol.11 , pp. 248-255
    • Varki, A.1
  • 106
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki A. Sialic acids in human health and disease. Trends Mol. Med. 2008, 14:351-360.
    • (2008) Trends Mol. Med. , vol.14 , pp. 351-360
    • Varki, A.1
  • 107
    • 70349296876 scopus 로고    scopus 로고
    • Human-specific evolution of sialic acid targets: explaining the malignant malaria mystery?
    • Varki A., Gagneux P. Human-specific evolution of sialic acid targets: explaining the malignant malaria mystery?. Proc. Natl. Acad. Sci. USA 2009, 106:14739-14740.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14739-14740
    • Varki, A.1    Gagneux, P.2
  • 108
    • 0017224180 scopus 로고
    • Eimeria tenella: host specificity in gallinaceous birds
    • Vetterling J.M. Eimeria tenella: host specificity in gallinaceous birds. J. Protozool. 1976, 23:155-158.
    • (1976) J. Protozool. , vol.23 , pp. 155-158
    • Vetterling, J.M.1
  • 109
    • 0024416519 scopus 로고
    • Plasmodium vivax interaction with the human Duffy blood group glycoprotein: identification of a parasite receptor-like protein
    • Wertheimer S.P., Barnwell J.W. Plasmodium vivax interaction with the human Duffy blood group glycoprotein: identification of a parasite receptor-like protein. Exp. Parasitol. 1989, 69:340-350.
    • (1989) Exp. Parasitol. , vol.69 , pp. 340-350
    • Wertheimer, S.P.1    Barnwell, J.W.2
  • 110
    • 67649537958 scopus 로고    scopus 로고
    • MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii
    • Zheng B., He A., Gan M., Li Z., He H., Zhan X. MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii. Parasitol. Res. 2009, 105:441-445.
    • (2009) Parasitol. Res. , vol.105 , pp. 441-445
    • Zheng, B.1    He, A.2    Gan, M.3    Li, Z.4    He, H.5    Zhan, X.6
  • 111
    • 2442690776 scopus 로고    scopus 로고
    • Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex
    • Zhou X.W., Blackman M.J., Howell S.A., Carruthers V.B. Proteomic analysis of cleavage events reveals a dynamic two-step mechanism for proteolysis of a key parasite adhesive complex. Mol. Cell. Proteomics 2004, 3:565-576.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 565-576
    • Zhou, X.W.1    Blackman, M.J.2    Howell, S.A.3    Carruthers, V.B.4


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