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Volumn 123, Issue 3, 2006, Pages 203-220

Glycobiology of Leishmania donovani

Author keywords

Anti O acetylated sialic acid antibodies; Complement pathway; Leishmania donovani; Lipophosphoglycan; O acetylated sialic acid; Phosphoglycan; Proteophosphoglycans; Sialic acid; Visceral leishmaniasis

Indexed keywords

ANTIBODY; ANTIMONY GLUCONATE; CELL SURFACE PROTEIN; COMPLEMENT MEMBRANE ATTACK COMPLEX; GLYCAN DERIVATIVE; GLYCOCONJUGATE; IMMUNOGLOBULIN M; LECTIN; LIPOPHOSPHOGLYCAN; PHOSPHOLIPID DERIVATIVE; SIALIC ACID DERIVATIVE; SIALOGLYCOPROTEIN;

EID: 33745216446     PISSN: 09715916     EISSN: 09715916     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (28)

References (76)
  • 1
    • 0037442697 scopus 로고    scopus 로고
    • Leishmaniasis: New approaches to disease control
    • Davies CR, Kaye P, Croft SL, Sundar S. Leishmaniasis: new approaches to disease control. BMJ 2003; 326 : 377-82.
    • (2003) BMJ , vol.326 , pp. 377-382
    • Davies, C.R.1    Kaye, P.2    Croft, S.L.3    Sundar, S.4
  • 2
    • 0032554330 scopus 로고    scopus 로고
    • Rapid accurate field diagnosis of Indian visceral leishmanisis
    • Sundar S, Reed SG, Singh VP, Kumar PC, Murray HW. Rapid accurate field diagnosis of Indian visceral leishmanisis. Lancet 1998; 351 : 563-5.
    • (1998) Lancet , vol.351 , pp. 563-565
    • Sundar, S.1    Reed, S.G.2    Singh, V.P.3    Kumar, P.C.4    Murray, H.W.5
  • 3
    • 0035949141 scopus 로고    scopus 로고
    • Treatment of Indian visceral leishmaniasis with single dose or daily infusion of low dose liposomal amphotericin B, a randomized trial
    • Sundar S, Agarwal G, Ria M, Murray HW. Treatment of Indian visceral leishmaniasis with single dose or daily infusion of low dose liposomal amphotericin B, a randomized trial. BMJ 2002; 323 : 419-22.
    • (2002) BMJ , vol.323 , pp. 419-422
    • Sundar, S.1    Agarwal, G.2    Ria, M.3    Murray, H.W.4
  • 4
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson MA. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J Cell Sci 1999; 112 : 2799-809.
    • (1999) J Cell Sci , vol.112 , pp. 2799-2809
    • Ferguson, M.A.1
  • 5
    • 0023664625 scopus 로고
    • Structure of the lipid moiety of the Leishmania donovani lipophosphoglycan
    • Orlandi PA Jr, Turco SJ. Structure of the lipid moiety of the Leishmania donovani lipophosphoglycan. J Biol Chem 1987; 262 : 10384-91.
    • (1987) J Biol Chem , vol.262 , pp. 10384-10391
    • Orlandi Jr., P.A.1    Turco, S.J.2
  • 6
    • 0025808065 scopus 로고
    • Developmental changes in the glycosylated phosphatidylinositols of Leishmania donovani. Characterization of the promastigote and amastigote glycolipids
    • McConville MJ, Blackwell JM. Developmental changes in the glycosylated phosphatidylinositols of Leishmania donovani. Characterization of the promastigote and amastigote glycolipids. J Biol Chem 1991; 266: 15170-9.
    • (1991) J Biol Chem , vol.266 , pp. 15170-15179
    • McConville, M.J.1    Blackwell, J.M.2
  • 7
    • 0027971162 scopus 로고
    • O- and N-glycosylation of the Leishmania mexicana-secreted acid phosphatase. Characterization of a new class of phosphoserine-linked glycans
    • Ilg T, Overath P, Ferguson MA, Rutherford T, Campbell DG, McConville MJ. O- and N-glycosylation of the Leishmania mexicana-secreted acid phosphatase. Characterization of a new class of phosphoserine-linked glycans. J Biol Chem 1994; 269 : 24073-81.
    • (1994) J Biol Chem , vol.269 , pp. 24073-24081
    • Ilg, T.1    Overath, P.2    Ferguson, M.A.3    Rutherford, T.4    Campbell, D.G.5    McConville, M.J.6
  • 8
    • 0027981027 scopus 로고
    • Characterization of phosphoglycan-containing secretory products of Leishmania
    • Ilg T, Stierhof YD, Wiese M, McConville MJ, Overath P. Characterization of phosphoglycan-containing secretory products of Leishmania. Parasitology 1994; 108 (Suppl): S63-71.
    • (1994) Parasitology , vol.108 , Issue.SUPPL.
    • Ilg, T.1    Stierhof, Y.D.2    Wiese, M.3    McConville, M.J.4    Overath, P.5
  • 9
    • 0029810396 scopus 로고    scopus 로고
    • Purification and structural characterization of a filamentous, mucin-like proteophosphoglycan secreted by Leishmania parasites
    • Ilg T, Stierhof YD, Craik D, Simpson R, Handman E, Bacic A. Purification and structural characterization of a filamentous, mucin-like proteophosphoglycan secreted by Leishmania parasites. J Biol Chem 1996; 271 : 21583-96.
    • (1996) J Biol Chem , vol.271 , pp. 21583-21596
    • Ilg, T.1    Stierhof, Y.D.2    Craik, D.3    Simpson, R.4    Handman, E.5    Bacic, A.6
  • 10
    • 0022992957 scopus 로고
    • Comparison of extracellular acid phosphatases from various isolates of Leishmania
    • Lovelace JK, Gottlieb M. Comparison of extracellular acid phosphatases from various isolates of Leishmania. Am J Trop Med Hyg 1986; 35: 1121-8.
    • (1986) Am J Trop Med Hyg , vol.35 , pp. 1121-1128
    • Lovelace, J.K.1    Gottlieb, M.2
  • 11
    • 0033615693 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel repeat-containing Leishmania major gene, ppg1, that encodes a membrane-associated form of proteophosphoglycan with a putative glycosylphosphatidylinositol anchor
    • Ilg T, Montgomery J, Stierhof YD, Handman E. Molecular cloning and characterization of a novel repeat-containing Leishmania major gene, ppg1, that encodes a membrane-associated form of proteophosphoglycan with a putative glycosylphosphatidylinositol anchor. J Biol Chem 1999; 274 : 31410-20.
    • (1999) J Biol Chem , vol.274 , pp. 31410-31420
    • Ilg, T.1    Montgomery, J.2    Stierhof, Y.D.3    Handman, E.4
  • 12
    • 0032826132 scopus 로고    scopus 로고
    • Proteophosphoglycans from Leishmania promastigotes and amastigotes
    • Ilg T, Handman E, Stierhof YD. Proteophosphoglycans from Leishmania promastigotes and amastigotes. Biochem Soc Trans 1999; 4 : 518-25.
    • (1999) Biochem Soc Trans , vol.4 , pp. 518-525
    • Ilg, T.1    Handman, E.2    Stierhof, Y.D.3
  • 13
    • 0026746610 scopus 로고
    • The lipophosphoglycan of Leishmania parasites
    • Turco SJ, Descoteaux A. The lipophosphoglycan of Leishmania parasites. Annu Rev Microbiol 1992; 46: 65-941.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 65-941
    • Turco, S.J.1    Descoteaux, A.2
  • 14
    • 0032852260 scopus 로고    scopus 로고
    • Glycoconjugates in Leishmania infectivity
    • Descoteaux A, Turco SJ. Glycoconjugates in Leishmania infectivity. Biochim Biophys Acta 1999; 1455 : 341-52.
    • (1999) Biochim Biophys Acta , vol.1455 , pp. 341-352
    • Descoteaux, A.1    Turco, S.J.2
  • 15
    • 0029118175 scopus 로고
    • Structure of Leishmania lipophosphoglycan: Inter- and intra-specific polymorphism in Old World species
    • McConville MJ, Schnur LF, Jaffe C, Schneider P. Structure of Leishmania lipophosphoglycan: inter- and intra-specific polymorphism in Old World species. Biochem J 1995; 310: 807-18.
    • (1995) Biochem J , vol.310 , pp. 807-818
    • McConville, M.J.1    Schnur, L.F.2    Jaffe, C.3    Schneider, P.4
  • 16
    • 0033572388 scopus 로고    scopus 로고
    • Characterization of the glucosyltransferases that assemble the side chains of the Indian Leishmania donovani lipophosphoglycan
    • Bray AE, Turco SJ. Characterization of the glucosyltransferases that assemble the side chains of the Indian Leishmania donovani lipophosphoglycan. Arch Biochem Biophys 1999; 372 : 367-74
    • (1999) Arch Biochem Biophys , vol.372 , pp. 367-374
    • Bray, A.E.1    Turco, S.J.2
  • 17
    • 0028963375 scopus 로고
    • Stage-specific binding of Leishmania donovani to the sand fly vector midgut is regulated by conformational changes in the abundant surface lipophosphoglycan
    • Sacks DL, Pimenta PF, McConville MJ, Schneider P, Turco SJ. Stage-specific binding of Leishmania donovani to the sand fly vector midgut is regulated by conformational changes in the abundant surface lipophosphoglycan. J Exp Med 1995; 181 : 685-97.
    • (1995) J Exp Med , vol.181 , pp. 685-697
    • Sacks, D.L.1    Pimenta, P.F.2    McConville, M.J.3    Schneider, P.4    Turco, S.J.5
  • 18
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville MJ, Ferguson MA. The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem J 1993; 294 : 305-24.
    • (1993) Biochem J , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 20
    • 0004679964 scopus 로고    scopus 로고
    • Glycoproteins of parasites
    • Montreul J, Vliegenhart JFG, Schachter H, editors. Elsevier Science, B.V
    • Turco SJ. Glycoproteins of parasites. In: Montreul J, Vliegenhart JFG, Schachter H, editors. Glycoproteins and disease. Elsevier Science, B.V., 1996 p. 113-24.
    • (1996) Glycoproteins and Disease , pp. 113-124
    • Turco, S.J.1
  • 21
    • 0024512492 scopus 로고
    • Inhibitory effects on Protein kinase C activity by lipophosphoglycan fragments and glycosylphosphatidyl inositol antigens on the protozoan parasite Leishmania
    • McNeely TB, Rosen G, Londner MV, Turco SJ. Inhibitory effects on Protein kinase C activity by lipophosphoglycan fragments and glycosylphosphatidyl inositol antigens on the protozoan parasite Leishmania. Biochem J 1989; 259 : 601-4.
    • (1989) Biochem J , vol.259 , pp. 601-604
    • McNeely, T.B.1    Rosen, G.2    Londner, M.V.3    Turco, S.J.4
  • 22
    • 0028935560 scopus 로고
    • Glycoinositolphospholipids of Leishmania major inhibit nitric oxide synthesis and reduce leishmanicidal activity in murine macrophages
    • Proudfoot L, O'Donnel CA, Liew FY. Glycoinositolphospholipids of Leishmania major inhibit nitric oxide synthesis and reduce leishmanicidal activity in murine macrophages. Eur J Immunol 1995; 25 : 745-50.
    • (1995) Eur J Immunol , vol.25 , pp. 745-750
    • Proudfoot, L.1    O'Donnel, C.A.2    Liew, F.Y.3
  • 23
    • 0030963611 scopus 로고    scopus 로고
    • Signal transduction in macrophage by glycosylphosphatidylinositol of Plasmodium, Trypanosoma and Leishmania; activation of protein tyrosine kinase and protein kinase by inositolglycan and diacylglycerol moiety
    • Tachado SD, Gerold P, Schwartz R, Novakovic S, McConville M, Schofield L. Signal transduction in macrophage by glycosylphosphatidylinositol of Plasmodium, Trypanosoma and Leishmania; activation of protein tyrosine kinase and protein kinase by inositolglycan and diacylglycerol moiety. Proc Natl Acad Sci USA 1997; 94 : 4022-7.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4022-4027
    • Tachado, S.D.1    Gerold, P.2    Schwartz, R.3    Novakovic, S.4    McConville, M.5    Schofield, L.6
  • 24
    • 0032785077 scopus 로고    scopus 로고
    • Specificity in signal transduction among glycosylphosphatidylinositols of Plasmodium falciparum, Trypanosome brucei, Trypanosome cruzi and Leishmania spp
    • Tachado SD, Mazhari-Tabrizi R, Schofield L. Specificity in signal transduction among glycosylphosphatidylinositols of Plasmodium falciparum, Trypanosome brucei, Trypanosome cruzi and Leishmania spp. Parasite Immunol 1999; 21 : 609-17.
    • (1999) Parasite Immunol , vol.21 , pp. 609-617
    • Tachado, S.D.1    Mazhari-Tabrizi, R.2    Schofield, L.3
  • 25
    • 0033577698 scopus 로고    scopus 로고
    • Evidence that free GPI glycolipids are essential for growth of Leishmania mexicana
    • Ilgoutz SC, Zawadzski J, Ralton JE, McConville MJ. Evidence that free GPI glycolipids are essential for growth of Leishmania mexicana. EMBO J 1999; 18 : 2746-55.
    • (1999) EMBO J , vol.18 , pp. 2746-2755
    • Ilgoutz, S.C.1    Zawadzski, J.2    Ralton, J.E.3    McConville, M.J.4
  • 26
    • 0024439986 scopus 로고
    • The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage
    • Medina-Acosta E, Kavess RE, Schwartz H, Russell DG. The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage. Mol Biochem Parasitol 1989; 37 : 263-73.
    • (1989) Mol Biochem Parasitol , vol.37 , pp. 263-273
    • Medina-Acosta, E.1    Kavess, R.E.2    Schwartz, H.3    Russell, D.G.4
  • 27
    • 0032529002 scopus 로고    scopus 로고
    • The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)
    • Schlagenhauf E, Etges R, Metcalf P. The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63). Structure 1998; 6 : 1035-46.
    • (1998) Structure , vol.6 , pp. 1035-1046
    • Schlagenhauf, E.1    Etges, R.2    Metcalf, P.3
  • 28
    • 0023837354 scopus 로고
    • Molecular cloning of the major surface antigen of Leishmania
    • Button LL, McMaster WR. Molecular cloning of the major surface antigen of Leishmania. J Exp Med 1988; 167: 724-9.
    • (1988) J Exp Med , vol.167 , pp. 724-729
    • Button, L.L.1    McMaster, W.R.2
  • 29
    • 0026533657 scopus 로고
    • The interaction of Leishmania species with macrophages
    • Alexander J, Russell DG. The interaction of Leishmania species with macrophages. Adv Parasitol 1992; 31 : 175-254.
    • (1992) Adv Parasitol , vol.31 , pp. 175-254
    • Alexander, J.1    Russell, D.G.2
  • 30
    • 0032826132 scopus 로고    scopus 로고
    • Proteophosphoglycans from Leishmania promastigotes and amastigotes
    • Ilg T, Handman E, Stierhof YD. Proteophosphoglycans from Leishmania promastigotes and amastigotes. Biochem Soc Trans 1999; 27 : 48-55.
    • (1999) Biochem Soc Trans , vol.27 , pp. 48-55
    • Ilg, T.1    Handman, E.2    Stierhof, Y.D.3
  • 31
    • 0025122358 scopus 로고
    • Golgi mediated post translational processing of secretory acid phosphatase by Leishmania donovani promastigotes
    • Bates PA, Hermes I, Dwyer DM. Golgi mediated post translational processing of secretory acid phosphatase by Leishmania donovani promastigotes. Mol Biochem. Parasitol 1990; 39 : 247-56.
    • (1990) Mol Biochem. Parasitol , vol.39 , pp. 247-256
    • Bates, P.A.1    Hermes, I.2    Dwyer, D.M.3
  • 32
    • 0028204437 scopus 로고
    • Characterization of polymer release from the flagellar pocket of Leishmania mexicana promastigotes
    • Stierhof YD, Ilg T, Russell DG, Hohenberg H, Overath P. Characterization of polymer release from the flagellar pocket of Leishmania mexicana promastigotes. J Cell Biol 1994; 125 : 321-31.
    • (1994) J Cell Biol , vol.125 , pp. 321-331
    • Stierhof, Y.D.1    Ilg, T.2    Russell, D.G.3    Hohenberg, H.4    Overath, P.5
  • 33
    • 0028861644 scopus 로고
    • Purification, partial characterization and immunolocalization of a proteophosphoglycan secreted by Leishmania mexicana amastigotes
    • Ilg T, Stierhof YD, McConville MJ, Overath P. Purification, partial characterization and immunolocalization of a proteophosphoglycan secreted by Leishmania mexicana amastigotes. Eur J Cell Biol 1995; 66 : 205-15.
    • (1995) Eur J Cell Biol , vol.66 , pp. 205-215
    • Ilg, T.1    Stierhof, Y.D.2    McConville, M.J.3    Overath, P.4
  • 34
    • 0023801906 scopus 로고
    • The ultrastructure of Leishmania major in the foregut and proboscis of Phlebotomus papatasi
    • Killick-Kendrick R, Wallbanks KR, Molyneux DH, Lavin DR. The ultrastructure of Leishmania major in the foregut and proboscis of Phlebotomus papatasi. Parasitol Res 1988; 74 : 586-90.
    • (1988) Parasitol Res , vol.74 , pp. 586-590
    • Killick-Kendrick, R.1    Wallbanks, K.R.2    Molyneux, D.H.3    Lavin, D.R.4
  • 35
    • 0030725428 scopus 로고    scopus 로고
    • Secreted proteophosphoglycan of Leishmania mexicana amastigotes activates complement by triggering the mannan binding lectin pathway
    • Peters C, Kawakami M, Kaul M, Ilg T, Overath P, Aebischer T. Secreted proteophosphoglycan of Leishmania mexicana amastigotes activates complement by triggering the mannan binding lectin pathway. Eur J Immunol 1997; 27 : 2666-72.
    • (1997) Eur J Immunol , vol.27 , pp. 2666-2672
    • Peters, C.1    Kawakami, M.2    Kaul, M.3    Ilg, T.4    Overath, P.5    Aebischer, T.6
  • 36
    • 0031020154 scopus 로고    scopus 로고
    • Proteophosphoglycan secreted by Leishmania mexicana amastigotes causes vacuole formation in macrophages
    • Peters C, Stierhof YD, Ilg T. Proteophosphoglycan secreted by Leishmania mexicana amastigotes causes vacuole formation in macrophages. Infect Immun 1997; 65 : 783-6.
    • (1997) Infect Immun , vol.65 , pp. 783-786
    • Peters, C.1    Stierhof, Y.D.2    Ilg, T.3
  • 37
    • 0038394488 scopus 로고    scopus 로고
    • Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes
    • Chatterjee M, Chava AK, Kohla G, Pal S, Merling A, Hinderlich S, et al. Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes. Glycobiology 2003; 5 : 351-61.
    • (2003) Glycobiology , vol.5 , pp. 351-361
    • Chatterjee, M.1    Chava, A.K.2    Kohla, G.3    Pal, S.4    Merling, A.5    Hinderlich, S.6
  • 39
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular interactions
    • Kelm S, Schauer R. Sialic acids in molecular and cellular interactions. Int Rev Cytol 1997; 175 : 137-240.
    • (1997) Int Rev Cytol , vol.175 , pp. 137-240
    • Kelm, S.1    Schauer, R.2
  • 40
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective
    • Angata T, Varki A. Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective. Chem Rev 2002; 102 : 439-69.
    • (2002) Chem Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 41
    • 0034444960 scopus 로고    scopus 로고
    • Achievements and challenges of sialic acid research
    • Schauer R, Achievements and challenges of sialic acid research. Glycoconj J 2000; 17 : 485-99.
    • (2000) Glycoconj J , vol.17 , pp. 485-499
    • Schauer, R.1
  • 42
    • 0031714484 scopus 로고    scopus 로고
    • A structural difference between the cell surfaces of humans and the great apes
    • Muchmore EA, Diaz S, Varki A. A structural difference between the cell surfaces of humans and the great apes. Am J Phys Anthropol 1998; 107: 187-98.
    • (1998) Am J Phys Anthropol , vol.107 , pp. 187-198
    • Muchmore, E.A.1    Diaz, S.2    Varki, A.3
  • 43
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • Schauer R. Chemistry, metabolism, and biological functions of sialic acids. Adv Carbohydr Chem Biochem 1982; 40 : 131-234.
    • (1982) Adv Carbohydr Chem Biochem , vol.40 , pp. 131-234
    • Schauer, R.1
  • 44
    • 0034664947 scopus 로고    scopus 로고
    • Identification of transient glycosylation alterations of sialylated mucin oligosaccharides during infection by the rat intestinal parasite Nippostrongylus brasiliensis
    • Karlsson NG, Olson FJ, Jovall PA, Andersch Y, Enerback L, Hansson GC. Identification of transient glycosylation alterations of sialylated mucin oligosaccharides during infection by the rat intestinal parasite Nippostrongylus brasiliensis. Biochem J 2000; 350 : 805-14.
    • (2000) Biochem J , vol.350 , pp. 805-814
    • Karlsson, N.G.1    Olson, F.J.2    Jovall, P.A.3    Andersch, Y.4    Enerback, L.5    Hansson, G.C.6
  • 45
    • 0023320997 scopus 로고
    • Fractionation of sialylated oligosaccharides, glycopeptides, and glycoproteins on immobilized elderberry (Sambucus nigra L.) bark lectin
    • Shibuya N, Goldstein IJ, Broekaert WF, Nsimba-Lubaki M, Peeters B, Peumans WJ. Fractionation of sialylated oligosaccharides, glycopeptides, and glycoproteins on immobilized elderberry (Sambucus nigra L.) bark lectin. Arch Biochem Biophys 1987; 254 : 1-8.
    • (1987) Arch Biochem Biophys , vol.254 , pp. 1-8
    • Shibuya, N.1    Goldstein, I.J.2    Broekaert, W.F.3    Nsimba-Lubaki, M.4    Peeters, B.5    Peumans, W.J.6
  • 46
    • 0024278423 scopus 로고
    • The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues
    • Wang WC, Cummings RD. The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues. J Biol Chem 1988; 263 : 4576-85.
    • (1988) J Biol Chem , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 47
    • 0028206055 scopus 로고
    • The oligosaccharide binding specificities of CD22 beta, a sialic acid-specific lectin of B cells
    • Powell LD, Varki A. The oligosaccharide binding specificities of CD22 beta, a sialic acid-specific lectin of B cells. J Biol Chem 1994; 269 : 10628-36.
    • (1994) J Biol Chem , vol.269 , pp. 10628-10636
    • Powell, L.D.1    Varki, A.2
  • 48
    • 0027511875 scopus 로고
    • Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition
    • Powell LD, Sgroi D, Sjoberg ER, Stamenkovic I, Varki A. Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition. J Biol Chem 1993; 268 : 7019-27.
    • (1993) J Biol Chem , vol.268 , pp. 7019-7027
    • Powell, L.D.1    Sgroi, D.2    Sjoberg, E.R.3    Stamenkovic, I.4    Varki, A.5
  • 49
    • 0038483141 scopus 로고    scopus 로고
    • Carbohydrates and lectin section report
    • Mason D, Andre P, Bensussan A, Buckley C, Civin C, Clark E, de Haas M, Goyert S, Hadam M, Hart D, Horejsi V, Jones Y, Mener S, Morrisey J, Schwartz-Albiez R, Shaw S, Simmons D, Turni L, Uguccioni M, van der Schoot E, Vivier E, Zola H, editors. New York: Oxford University Press
    • Schwartz-Albiez R. Carbohydrates and lectin section report. In: Mason D, Andre P, Bensussan A, Buckley C, Civin C, Clark E, de Haas M, Goyert S, Hadam M, Hart D, Horejsi V, Jones Y, Mener S, Morrisey J, Schwartz-Albiez R, Shaw S, Simmons D, Turni L, Uguccioni M, van der Schoot E, Vivier E, Zola H, editors. Leucocyte typing VII. New York: Oxford University Press; 2002 p. 149-64.
    • (2002) Leucocyte Typing VII , pp. 149-164
    • Schwartz-Albiez, R.1
  • 50
    • 0037147257 scopus 로고    scopus 로고
    • Cloning of Trypanosoma brucei and Leishmania major genes encoding the GlcNAc-phosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol biosynthesis that is essential to the African sleeping sickness parasite
    • Chang T, Milne KG, Guther ML, Smith TK, Ferguson MA. Cloning of Trypanosoma brucei and Leishmania major genes encoding the GlcNAc-phosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol biosynthesis that is essential to the African sleeping sickness parasite. J Biol Chem 2002; 277 : 50176-82.
    • (2002) J Biol Chem , vol.277 , pp. 50176-50182
    • Chang, T.1    Milne, K.G.2    Guther, M.L.3    Smith, T.K.4    Ferguson, M.A.5
  • 51
    • 0026752091 scopus 로고
    • Biosynthesis of lipophosphoglycan from Leishmania donovani: Characterization of mannosylphosphate transfer in vitro
    • Carver MA, Turco SJ. Biosynthesis of lipophosphoglycan from Leishmania donovani: characterization of mannosylphosphate transfer in vitro. Arch Biochem Biophys 1992; 295 : 309-17.
    • (1992) Arch Biochem Biophys , vol.295 , pp. 309-317
    • Carver, M.A.1    Turco, S.J.2
  • 52
    • 0032128405 scopus 로고    scopus 로고
    • Leishmania donovani has distinct mannosylphosphoryltransferases for the initiation and elongation phases of lipophosphoglycan repeating unit biosynthesis
    • Descoteaux A, Mengeling BJ, Beverley SM, Turco SJ. Leishmania donovani has distinct mannosylphosphoryltransferases for the initiation and elongation phases of lipophosphoglycan repeating unit biosynthesis. Mol Biochem Parasitol 1998; 94 : 27-40.
    • (1998) Mol Biochem Parasitol , vol.94 , pp. 27-40
    • Descoteaux, A.1    Mengeling, B.J.2    Beverley, S.M.3    Turco, S.J.4
  • 54
    • 0033046601 scopus 로고    scopus 로고
    • Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus
    • Keppler OT, Peter ME, Hinderlich S, Moldenhauer G, Stehling P, Schmitz I, et al. Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/ Fas)-mediated apoptosis and for infection by a lymphotropic virus. Glycobiology 1999; 9 : 557-69.
    • (1999) Glycobiology , vol.9 , pp. 557-569
    • Keppler, O.T.1    Peter, M.E.2    Hinderlich, S.3    Moldenhauer, G.4    Stehling, P.5    Schmitz, I.6
  • 55
    • 0023447901 scopus 로고
    • Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi
    • Zingales B, Carniol C, de Lederkremer RM, Colli W. Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi. Mol Biochem Parasitol 1987; 26 : 135-44.
    • (1987) Mol Biochem Parasitol , vol.26 , pp. 135-144
    • Zingales, B.1    Carniol, C.2    de Lederkremer, R.M.3    Colli, W.4
  • 56
    • 0029006744 scopus 로고
    • Distribution of developmentally regulated trans-sialidases in the Kinetoplastida and characterization of a shed trans-sialidase activity from procyclic Trypanosoma congolense
    • Engstler M, Schauer R, Brun R. Distribution of developmentally regulated trans-sialidases in the Kinetoplastida and characterization of a shed trans-sialidase activity from procyclic Trypanosoma congolense. Acta Trop 1995; 59 : 117-29.
    • (1995) Acta Trop , vol.59 , pp. 117-129
    • Engstler, M.1    Schauer, R.2    Brun, R.3
  • 57
    • 0030050069 scopus 로고    scopus 로고
    • Developmental differentiation between tachyzoites and bradyzoites of Toxoplasma gondii
    • Gross U, Bohne W, Soete M, Dubremetz JF. Developmental differentiation between tachyzoites and bradyzoites of Toxoplasma gondii. Parasitol Today 1996; 12 : 30-3.
    • (1996) Parasitol Today , vol.12 , pp. 30-33
    • Gross, U.1    Bohne, W.2    Soete, M.3    Dubremetz, J.F.4
  • 58
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson MA. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J Cell Sci 1999; 112 : 2799-809.
    • (1999) J Cell Sci , vol.112 , pp. 2799-2809
    • Ferguson, M.A.1
  • 60
    • 0027672713 scopus 로고
    • Leishmania-macrophage interactions: Multiple receptors, multiple ligands and diverse cellular responses
    • Mosser DM, Rosenthal LA. Leishmania-macrophage interactions: multiple receptors, multiple ligands and diverse cellular responses. Semin Cell Biol 1993; 4 : 315-22.
    • (1993) Semin Cell Biol , vol.4 , pp. 315-322
    • Mosser, D.M.1    Rosenthal, L.A.2
  • 61
    • 5444221208 scopus 로고    scopus 로고
    • Purification, characterization of O-acetylated sialoglycoconjugates-specific IgM, and development of an enzyme-linked immunosorbent assay for diagnosis and follow-up of indian visceral leishmaniasis patients
    • Bandyopadhyay S, Chatterjee M, Pal S, Waller RF, Sundar S, McConville MJ, et al. Purification, characterization of O-acetylated sialoglycoconjugates-specific IgM, and development of an enzyme-linked immunosorbent assay for diagnosis and follow-up of indian visceral leishmaniasis patients. Diagn Microbiol Infect Dis 2004; 50 : 15-24.
    • (2004) Diagn Microbiol Infect Dis , vol.50 , pp. 15-24
    • Bandyopadhyay, S.1    Chatterjee, M.2    Pal, S.3    Waller, R.F.4    Sundar, S.5    McConville, M.J.6
  • 62
    • 9444297936 scopus 로고    scopus 로고
    • Antibodies directed against O-acetylated sialoglycoconjugates accelerates complement activation in Leishmania donovani promastigotes
    • Bandyopadhyay S, Chatterjee M, Das T, Bandyopadhyay S, Sundar S, Mandal C. Antibodies directed against O-acetylated sialoglycoconjugates accelerates complement activation in Leishmania donovani promastigotes. J Infect Dis 2004; 190 : 2010-9.
    • (2004) J Infect Dis , vol.190 , pp. 2010-2019
    • Bandyopadhyay, S.1    Chatterjee, M.2    Das, T.3    Bandyopadhyay, S.4    Sundar, S.5    Mandal, C.6
  • 63
    • 0029907917 scopus 로고    scopus 로고
    • Effect of amplification of the Cap b locus on complement-mediated bacteriolysis and opsonization of type B Haemophilus influenzae
    • Noel GJ, Brittingham A, Granato AA, Mosser DM. Effect of amplification of the Cap b locus on complement-mediated bacteriolysis and opsonization of type B Haemophilus influenzae. Infect Immun 1996; 64 : 4769-75.
    • (1996) Infect Immun , vol.64 , pp. 4769-4775
    • Noel, G.J.1    Brittingham, A.2    Granato, A.A.3    Mosser, D.M.4
  • 65
    • 0037128162 scopus 로고    scopus 로고
    • Complement interaction with trypanosomatid promastigotes in normal human serum
    • Dominguez M, Moreno I, Lopez-Trascasa M, Torano A. Complement interaction with trypanosomatid promastigotes in normal human serum. J Exp Med 2002; 195 : 451-9.
    • (2002) J Exp Med , vol.195 , pp. 451-459
    • Dominguez, M.1    Moreno, I.2    Lopez-Trascasa, M.3    Torano, A.4
  • 66
    • 0021933722 scopus 로고
    • Cytotoxicity of human serum for Leishmania donovani amastigotes: Antibody facilitation of alternate complement pathway-mediated killing
    • Hoover DL, Berger M, Oppenheim MH, Hockmeyer WT, Meltzer MS. Cytotoxicity of human serum for Leishmania donovani amastigotes: antibody facilitation of alternate complement pathway-mediated killing. Infect Immun 1985; 47 : 247-52.
    • (1985) Infect Immun , vol.47 , pp. 247-252
    • Hoover, D.L.1    Berger, M.2    Oppenheim, M.H.3    Hockmeyer, W.T.4    Meltzer, M.S.5
  • 67
    • 0024506180 scopus 로고
    • Effect of immunoglobulin M from normal human serum on Leishmania donovani promastigote agglutination, complement-mediated killing, and phagocytosis by human monocytes
    • Navin TR, Krug EC, Pearson RD. Effect of immunoglobulin M from normal human serum on Leishmania donovani promastigote agglutination, complement-mediated killing, and phagocytosis by human monocytes. Infect Immun 1989; 57 : 1343-6.
    • (1989) Infect Immun , vol.57 , pp. 1343-1346
    • Navin, T.R.1    Krug, E.C.2    Pearson, R.D.3
  • 68
    • 3543127655 scopus 로고    scopus 로고
    • Sialoglycans in protozoal diseases: Their detection, modes of acquisition and emerging biological roles
    • Chava AK, Bandyopadhyay S, Chatterjee M, Mandal C. Sialoglycans in protozoal diseases: their detection, modes of acquisition and emerging biological roles. Glycoconjugate J 2004; 20 : 199-206.
    • (2004) Glycoconjugate J , vol.20 , pp. 199-206
    • Chava, A.K.1    Bandyopadhyay, S.2    Chatterjee, M.3    Mandal, C.4
  • 69
    • 0034431023 scopus 로고    scopus 로고
    • Role of linkage specific 9-O-acetylated sialoglycoconjugates in activation of the alternative complement pathway in mammalian erythrocytes
    • Sharma V, Chatterjee M, Sen G, Chava. AK, Mandal C. Role of linkage specific 9-O-acetylated sialoglycoconjugates in activation of the alternative complement pathway in mammalian erythrocytes. Glycoconjugate J 2000; 17 : 887-93.
    • (2000) Glycoconjugate J , vol.17 , pp. 887-893
    • Sharma, V.1    Chatterjee, M.2    Sen, G.3    Chava, A.K.4    Mandal, C.5
  • 70
    • 1842607674 scopus 로고    scopus 로고
    • Variable degree of alternative complement pathway-mediated hemolysis in Indian visceral leishmaniasis induced by differential expression of 9-O-acetylated sialoglycans
    • Chava AK, Chatterjee M, Sharma V, Sundar S, Mandal C. Variable degree of alternative complement pathway-mediated hemolysis in Indian visceral leishmaniasis induced by differential expression of 9-O-acetylated sialoglycans. J Infect Dis 2004; 189 : 1257-64.
    • (2004) J Infect Dis , vol.189 , pp. 1257-1264
    • Chava, A.K.1    Chatterjee, M.2    Sharma, V.3    Sundar, S.4    Mandal, C.5
  • 71
    • 0018820356 scopus 로고
    • An autosomal dominant gene regulates the extent of 9-O-acetylation of murine erythrocyte sialic acids. A probable explanation for the variation in capacity to activate the human alternative complement pathway
    • Varki A, Kornfeld S. An autosomal dominant gene regulates the extent of 9-O-acetylation of murine erythrocyte sialic acids. A probable explanation for the variation in capacity to activate the human alternative complement pathway. J Exp Med 1980; 152 : 532-44.
    • (1980) J Exp Med , vol.152 , pp. 532-544
    • Varki, A.1    Kornfeld, S.2
  • 72
    • 0031914961 scopus 로고    scopus 로고
    • Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup B
    • Jack DL, Dodds AW, Anwar N, Ison CA, Law A, Frosch M, et al. Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup B. J Immunol 1998; 160 : 1346-53.
    • (1998) J Immunol , vol.160 , pp. 1346-1353
    • Jack, D.L.1    Dodds, A.W.2    Anwar, N.3    Ison, C.A.4    Law, A.5    Frosch, M.6
  • 73
    • 0037090274 scopus 로고    scopus 로고
    • Regulation of the mannan-binding lectin pathway of complement on Neisseria gonorrhoeae by C1 - Inhibitor and alpha 2-macroglobulin
    • Gulati S, Sastry K, Jensenius JC, Rice PA, Ram S. Regulation of the mannan-binding lectin pathway of complement on Neisseria gonorrhoeae by C1 - inhibitor and alpha 2-macroglobulin. J Immunol 2002; 168: 4078-86.
    • (2002) J Immunol , vol.168 , pp. 4078-4086
    • Gulati, S.1    Sastry, K.2    Jensenius, J.C.3    Rice, P.A.4    Ram, S.5
  • 74
    • 0034012169 scopus 로고    scopus 로고
    • Mucin-like molecules form a negatively charged coat that protects Trypanosoma cruzi trypomastigotes from killing by human anti-alpha-galactosyl antibodies
    • Pereira-Chioccola VL, Acosta-Serrano A, Correia de Almeida I, Ferguson MA, Souto-Padron T, Rodrigues MM, et al. Mucin-like molecules form a negatively charged coat that protects Trypanosoma cruzi trypomastigotes from killing by human anti-alpha-galactosyl antibodies. J Cell Sci 2000; 113 : 1299-07.
    • (2000) J Cell Sci , vol.113 , pp. 1299-1307
    • Pereira-Chioccola, V.L.1    Acosta-Serrano, A.2    Correia de Almeida, I.3    Ferguson, M.A.4    Souto-Padron, T.5    Rodrigues, M.M.6
  • 75
    • 0033766338 scopus 로고    scopus 로고
    • Investigation of 9-O-acetylated sialoglycoconjugates in childhood acute lymphoblastic leukaemia
    • Mandal C, Chatterjee M, Sinha D. Investigation of 9-O-acetylated sialoglycoconjugates in childhood acute lymphoblastic leukaemia. Br J Haematol 2000; 110 : 801-12.
    • (2000) Br J Haematol , vol.110 , pp. 801-812
    • Mandal, C.1    Chatterjee, M.2    Sinha, D.3
  • 76
    • 0031899115 scopus 로고    scopus 로고
    • O-acetylation of sialic acids
    • Klein A, Roussel P. O-acetylation of sialic acids. Biochimie 1998; 80 : 49-57.
    • (1998) Biochimie , vol.80 , pp. 49-57
    • Klein, A.1    Roussel, P.2


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