메뉴 건너뛰기




Volumn 2, Issue 6, 2007, Pages 615-623

Pathobiology of virus glycosylation: Implications to disease and prospects for treatment

Author keywords

Antivirals; Glycosylation; Pharmacognosy; Virus

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; CD4 ANTIGEN; CHLOROQUINE; CONCANAVALIN A; CYANOVIRIN N; GALANTHUS NIVALIA EXTRACT; GLYCOPROTEIN GP 120; GLYCOSIDASE INHIBITOR; NEUTRALIZING ANTIBODY; OLIGOSACCHARIDE; PLANT EXTRACT; PLANT LECTIN; PRADIMICIN A; PROTEINASE; SURFACTANT PROTEIN D; UNCLASSIFIED DRUG; URTICA DIOICA EXTRACT; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS HEMAGGLUTININ; VIRUS SIALIDASE;

EID: 36348969551     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/17460794.2.6.615     Document Type: Review
Times cited : (2)

References (86)
  • 1
    • 34250854515 scopus 로고    scopus 로고
    • Essential role of Dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation
    • Mondotte JA, Lozach PY, Amara A, Gamarnik AV: Essential role of Dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation. J. Virol. 81, 7136-7148 (2007).
    • (2007) J. Virol , vol.81 , pp. 7136-7148
    • Mondotte, J.A.1    Lozach, P.Y.2    Amara, A.3    Gamarnik, A.V.4
  • 3
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S et al.: Antibody neutralization and escape by HIV-1. Nature 422, 307-312 (2003).
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3
  • 4
    • 0034845609 scopus 로고    scopus 로고
    • Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulu
    • Land A, Braakman I: Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulu. Biochimie 83, 783-790 (2001).
    • (2001) Biochimie , vol.83 , pp. 783-790
    • Land, A.1    Braakman, I.2
  • 5
    • 1242293619 scopus 로고    scopus 로고
    • HCV E2 glycoprotein: Mutagenesis of N-linked glycosylation sites and its effects on E2 expression and processing
    • Slater-Handshy T, Droll DA, Fan X, Di Bisceglie AM, Chambers TJ: HCV E2 glycoprotein: mutagenesis of N-linked glycosylation sites and its effects on E2 expression and processing. Virology 319, 36-48 (2004).
    • (2004) Virology , vol.319 , pp. 36-48
    • Slater-Handshy, T.1    Droll, D.A.2    Fan, X.3    Di Bisceglie, A.M.4    Chambers, T.J.5
  • 6
    • 0032898289 scopus 로고    scopus 로고
    • Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex
    • Meunier JC, Foumillier A, Choukhi A et al.: Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex. J. Gen. Virol. 80 (Pt 4), 887-896 (1999).
    • (1999) J. Gen. Virol , vol.80 , Issue.PART 4 , pp. 887-896
    • Meunier, J.C.1    Foumillier, A.2    Choukhi, A.3
  • 7
    • 0033934134 scopus 로고    scopus 로고
    • Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: A study by reverse genetics
    • Wagner R, Wolff T, Herwig A, Pleschka S, Klenk HD: Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J. Virol. 74, 6316-6323 (2000).
    • (2000) J. Virol , vol.74 , pp. 6316-6323
    • Wagner, R.1    Wolff, T.2    Herwig, A.3    Pleschka, S.4    Klenk, H.D.5
  • 8
    • 0037196586 scopus 로고    scopus 로고
    • Importance of hemagglutinin glycosylation for the biological functions of influenza virus
    • Klenk HD, Wagner R, Heuer D, Wolff T: Importance of hemagglutinin glycosylation for the biological functions of influenza virus. Virus Res. 82, 73-75 (2002).
    • (2002) Virus Res , vol.82 , pp. 73-75
    • Klenk, H.D.1    Wagner, R.2    Heuer, D.3    Wolff, T.4
  • 9
    • 0035813039 scopus 로고    scopus 로고
    • Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture
    • Baigent SJ, McCauley JW: Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture. Virus Res. 79, 177-185 (2001).
    • (2001) Virus Res , vol.79 , pp. 177-185
    • Baigent, S.J.1    McCauley, J.W.2
  • 10
    • 0036936397 scopus 로고    scopus 로고
    • Role of overlapping glycosylation sequons in antigenic properties, intracellular transport and biological activities of influenza A/H2N2 virus haemagglutinin
    • Tsuchiya E, Sugawara K, Hongo S, Matsuzaki Y, Muraki Y, Nakamura K: Role of overlapping glycosylation sequons in antigenic properties, intracellular transport and biological activities of influenza A/H2N2 virus haemagglutinin. J. Gen. Virol. 83, 3067-3074 (2002).
    • (2002) J. Gen. Virol , vol.83 , pp. 3067-3074
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3    Matsuzaki, Y.4    Muraki, Y.5    Nakamura, K.6
  • 11
    • 0036255966 scopus 로고    scopus 로고
    • Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule
    • Tsuchiya E, Sugawara K, Hongo S et al.: Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule. J. Gen. Virol. 83, 1137-1146 (2002).
    • (2002) J. Gen. Virol , vol.83 , pp. 1137-1146
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3
  • 12
    • 4444376554 scopus 로고    scopus 로고
    • Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin
    • Abe Y, Takashita E, Sugawara K, Matsuzaki Y, Muraki Y, Hongo S: Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin. J. Virol. 78, 9605-9611 (2004).
    • (2004) J. Virol , vol.78 , pp. 9605-9611
    • Abe, Y.1    Takashita, E.2    Sugawara, K.3    Matsuzaki, Y.4    Muraki, Y.5    Hongo, S.6
  • 13
    • 0036771639 scopus 로고    scopus 로고
    • Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants
    • Kaverin NV, Rudeva IA, Ilyushina NA et al.: Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants. J. Gen. Virol. 83, 2497-2505 (2002).
    • (2002) J. Gen. Virol , vol.83 , pp. 2497-2505
    • Kaverin, N.V.1    Rudeva, I.A.2    Ilyushina, N.A.3
  • 14
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R, Kurowski B, Johnson AE, Hebert DN: N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell 11, 79-90 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 15
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC: Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569 (2000).
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 17
    • 1842345479 scopus 로고
    • Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence
    • Deshpande KL, Fried VA, Ando M, Webster RG: Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Proc. Natl Acad. Sci. USA 84, 36-40 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 36-40
    • Deshpande, K.L.1    Fried, V.A.2    Ando, M.3    Webster, R.G.4
  • 18
    • 0032712272 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of influenza
    • Zambon MC: Epidemiology and pathogenesis of influenza. J. Antimicrob. Chemother. 44(Suppl. B), S3-S9 (1999).
    • (1999) J. Antimicrob. Chemother , vol.44 , Issue.SUPPL. B
    • Zambon, M.C.1
  • 19
    • 0027470149 scopus 로고
    • Expression of the G glycoprotein gene of human respiratory syncytial virus in Salmonella typhimurium
    • Martin-Gallardo A, Fleischer E, Doyle SA et al.: Expression of the G glycoprotein gene of human respiratory syncytial virus in Salmonella typhimurium. J. Gen. Virol. 74(Pt 3), 453-458 (1993).
    • (1993) J. Gen. Virol , vol.74 , Issue.PART 3 , pp. 453-458
    • Martin-Gallardo, A.1    Fleischer, E.2    Doyle, S.A.3
  • 20
    • 0026518657 scopus 로고
    • Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: Altered O-glycosylation in the presence of brefeldin A
    • Collins PL, Mottet G: Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A. J. Gen. Virol. 73(Pt 4), 849-863 (1992).
    • (1992) J. Gen. Virol , vol.73 , Issue.PART 4 , pp. 849-863
    • Collins, P.L.1    Mottet, G.2
  • 21
    • 33646447520 scopus 로고    scopus 로고
    • N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and vital entry
    • Aguilar HC, Matreyek KA, Filone CM et al.: N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and vital entry. J. Virol. 80, 4878-4889 (2006).
    • (2006) J. Virol , vol.80 , pp. 4878-4889
    • Aguilar, H.C.1    Matreyek, K.A.2    Filone, C.M.3
  • 22
    • 2942647917 scopus 로고    scopus 로고
    • Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein
    • Moll M, Kaufmann A, Maisner A: Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein. J. Virol. 78, 7274-7278 (2004).
    • (2004) J. Virol , vol.78 , pp. 7274-7278
    • Moll, M.1    Kaufmann, A.2    Maisner, A.3
  • 23
    • 21044446226 scopus 로고    scopus 로고
    • Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus
    • Bossart KN, Crameri G, Dimitrov AS et al.: Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus. J. Virol. 79, 6690-6702 (2005).
    • (2005) J. Virol , vol.79 , pp. 6690-6702
    • Bossart, K.N.1    Crameri, G.2    Dimitrov, A.S.3
  • 24
    • 33144477169 scopus 로고    scopus 로고
    • Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M
    • Oostra M, de Haan CA, de Groot RJ, Rottier PJ: Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M. J. Virol. 80, 2326-2336 (2006).
    • (2006) J. Virol , vol.80 , pp. 2326-2336
    • Oostra, M.1    de Haan, C.A.2    de Groot, R.J.3    Rottier, P.J.4
  • 25
    • 33750698660 scopus 로고    scopus 로고
    • Characterization of human metapneumovirus F protein-promoted membrane fusion: Critical roles for proteolytic processing and low Ph
    • Schowalter RM, Smith SE, Dutch RE: Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low Ph. J. Virol. 80(22), 10931-10941 (2006).
    • (2006) J. Virol , vol.80 , Issue.22 , pp. 10931-10941
    • Schowalter, R.M.1    Smith, S.E.2    Dutch, R.E.3
  • 26
    • 0034625771 scopus 로고    scopus 로고
    • Timing the ancestor of the HIV-1 pandemic strains
    • Korber B, Muldoon M, Theiler J et al.: Timing the ancestor of the HIV-1 pandemic strains. Science 288, 1789-1796 (2000).
    • (2000) Science , vol.288 , pp. 1789-1796
    • Korber, B.1    Muldoon, M.2    Theiler, J.3
  • 27
    • 0025331559 scopus 로고
    • Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1
    • Fenouillet E, Gluckman JC, Bahraoui E: Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1. J. Virol. 64, 2841-2848 (1990).
    • (1990) J. Virol , vol.64 , pp. 2841-2848
    • Fenouillet, E.1    Gluckman, J.C.2    Bahraoui, E.3
  • 28
    • 0001197838 scopus 로고
    • Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1
    • Montefiori DC, Robinson WE Jr, Mitchell WM: Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. Proc. Natl Acad. Sci. USA 85, 9248-9252 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 9248-9252
    • Montefiori, D.C.1    Robinson Jr, W.E.2    Mitchell, W.M.3
  • 29
    • 33748881797 scopus 로고    scopus 로고
    • N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization
    • Wolk T, Schreiber M: N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization. Med. Microbiol. Immunol. (Berl) 195, 165-172 (2006).
    • (2006) Med. Microbiol. Immunol. (Berl) , vol.195 , pp. 165-172
    • Wolk, T.1    Schreiber, M.2
  • 30
    • 33748881797 scopus 로고    scopus 로고
    • N-Glycans in the gp120 V1/V2 domain ofthe HIV-1 strain NL4-3 are indispensable for vital infectivity and resistance against antibody neutralization
    • Wolk T, Schreiber M: N-Glycans in the gp120 V1/V2 domain ofthe HIV-1 strain NL4-3 are indispensable for vital infectivity and resistance against antibody neutralization. Med. Microbiol. Immunol. 195, 165-172 (2006).
    • (2006) Med. Microbiol. Immunol , vol.195 , pp. 165-172
    • Wolk, T.1    Schreiber, M.2
  • 31
    • 0027957921 scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoproteinis modified by O-linked oligosaccharides
    • Bernstein HB, Tucker SP, Hunter E, Schutzbach JS, Compans RW: Human immunodeficiency virus type 1 envelope glycoproteinis modified by O-linked oligosaccharides. J. Virol. 68, 463-468 (1994).
    • (1994) J. Virol , vol.68 , pp. 463-468
    • Bernstein, H.B.1    Tucker, S.P.2    Hunter, E.3    Schutzbach, J.S.4    Compans, R.W.5
  • 32
    • 0024355330 scopus 로고
    • Glycoproteins: What are the sugar chains for?
    • Paulson JC: Glycoproteins: what are the sugar chains for? Trends Biochem. Sci. 14, 272-276 (1989).
    • (1989) Trends Biochem. Sci , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 33
    • 0036719574 scopus 로고    scopus 로고
    • Antibodies, viruses and vaccines
    • Burton DR: Antibodies, viruses and vaccines. Nat. Rev. Immunol. 2, 706-713 (2002).
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 706-713
    • Burton, D.R.1
  • 34
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders RW, Venturi M, Schiffner L et al.: The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 76, 7293-7305 (2002).
    • (2002) J. Virol , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3
  • 35
    • 34547808791 scopus 로고    scopus 로고
    • In vivo and in vitro escape from neutralizing antibodies 2G12, 2F5, and 4E10
    • Manrique A, Rusert P, Joos B et al.: In vivo and in vitro escape from neutralizing antibodies 2G12, 2F5, and 4E10. J. Virol. 81, 8793-8808 (2007).
    • (2007) J. Virol , vol.81 , pp. 8793-8808
    • Manrique, A.1    Rusert, P.2    Joos, B.3
  • 36
    • 26444450696 scopus 로고    scopus 로고
    • Dissection of the carbohydrate specificity of the broadly neutralizing and-HIV-1 antibody 2G12
    • Calarese DA, Lee HK, Huang CY et al.: Dissection of the carbohydrate specificity of the broadly neutralizing and-HIV-1 antibody 2G12. Proc. Natl Acad. Sci. USA 102, 13372-13377 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13372-13377
    • Calarese, D.A.1    Lee, H.K.2    Huang, C.Y.3
  • 37
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, Scanlan CN, Zwick MB et al.: Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300, 2065-2071 (2003).
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1    Scanlan, C.N.2    Zwick, M.B.3
  • 38
    • 0038407687 scopus 로고    scopus 로고
    • DC-SIGN: A novel HIV receptor on DCs that mediates HIV-1 transmission
    • Geijtenbeek TB, van Kooyk Y: DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission. Curr. Top Microbiol. Immunol. 276, 31-54 (2003).
    • (2003) Curr. Top Microbiol. Immunol , vol.276 , pp. 31-54
    • Geijtenbeek, T.B.1    van Kooyk, Y.2
  • 39
    • 16844372394 scopus 로고    scopus 로고
    • HIV-1 Nef mediates post-translational down-regulation and redistribution of the mannose receptor
    • Vigerust DJ, Egan BS, Shepherd VL: HIV-1 Nef mediates post-translational down-regulation and redistribution of the mannose receptor. J. Leukoc. Biol. 77, 522-534 (2005).
    • (2005) J. Leukoc. Biol , vol.77 , pp. 522-534
    • Vigerust, D.J.1    Egan, B.S.2    Shepherd, V.L.3
  • 40
    • 34247570415 scopus 로고    scopus 로고
    • Noninfectious entry of HIV-1 into peripheral and brain macrophages mediated by the mannose receptor
    • Trujillo JR, Rogers R, Molina RM et al.: Noninfectious entry of HIV-1 into peripheral and brain macrophages mediated by the mannose receptor. Poc. Natl Acad. Sci. USA 104, 5097-5102 (2007).
    • (2007) Poc. Natl Acad. Sci. USA , vol.104 , pp. 5097-5102
    • Trujillo, J.R.1    Rogers, R.2    Molina, R.M.3
  • 41
    • 29444442970 scopus 로고    scopus 로고
    • Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection
    • Frost SD, Wrin T, Smith DM et al.: Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection. Proc. Natl Acad. Sci. USA 102, 18514-18519 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18514-18519
    • Frost, S.D.1    Wrin, T.2    Smith, D.M.3
  • 42
    • 0034469170 scopus 로고    scopus 로고
    • The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors
    • Malenbaum SE, Yang D, Cavacini L, Posner M, Robinson J, Cheng-Mayer C: The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors. J. Virol. 74, 11008-11016 (2000).
    • (2000) J. Virol , vol.74 , pp. 11008-11016
    • Malenbaum, S.E.1    Yang, D.2    Cavacini, L.3    Posner, M.4    Robinson, J.5    Cheng-Mayer, C.6
  • 43
    • 7444256169 scopus 로고    scopus 로고
    • Genetic diversity and evolution of hepatitis C virus - 15 years on
    • Simmonds P: Genetic diversity and evolution of hepatitis C virus - 15 years on. J. Gen. Virol. 85, 3173-3188 (2004).
    • (2004) J. Gen. Virol , vol.85 , pp. 3173-3188
    • Simmonds, P.1
  • 44
    • 9944256449 scopus 로고    scopus 로고
    • Viral envelope protein glycosylation is a molecular determinant of the neuroinvasiveness of the New York strain of West Nile virus
    • Shirato K, Miyoshi H, Goto A et al.: Viral envelope protein glycosylation is a molecular determinant of the neuroinvasiveness of the New York strain of West Nile virus. J. Gen. Virol. 85, 3637-3645 (2004).
    • (2004) J. Gen. Virol , vol.85 , pp. 3637-3645
    • Shirato, K.1    Miyoshi, H.2    Goto, A.3
  • 45
    • 0035680497 scopus 로고    scopus 로고
    • Biological significance of glycosylation of the envelope protein of Kunjin virus
    • Scherret JH, Mackenzie JSs, Khromykh AA, Hall RA: Biological significance of glycosylation of the envelope protein of Kunjin virus. Ann. NY Acad. Sci. 951, 361-363 (2001).
    • (2001) Ann. NY Acad. Sci , vol.951 , pp. 361-363
    • Scherret, J.H.1    Mackenzie, J.S.2    Khromykh, A.A.3    Hall, R.A.4
  • 46
    • 20744441654 scopus 로고    scopus 로고
    • Envelope protein glycosylation status influences mouse neuroinvasion phenotype of genetic lineage 1 West Nile virus strains
    • Beasley DW, Whiteman MC, Zhang S et al.: Envelope protein glycosylation status influences mouse neuroinvasion phenotype of genetic lineage 1 West Nile virus strains. J. Virol. 79, 8339-8347 (2005).
    • (2005) J. Virol , vol.79 , pp. 8339-8347
    • Beasley, D.W.1    Whiteman, M.C.2    Zhang, S.3
  • 47
    • 0034463839 scopus 로고    scopus 로고
    • Effect of tunicamycin on expression of epitopes on Japanese encephalitis virus glycoprotein E in porcine kidney cells
    • Lad VJ, Shende VR, Gupta AK, Koshy AA, Roy A: Effect of tunicamycin on expression of epitopes on Japanese encephalitis virus glycoprotein E in porcine kidney cells. Acta Virol. 44, 359-364 (2000).
    • (2000) Acta Virol , vol.44 , pp. 359-364
    • Lad, V.J.1    Shende, V.R.2    Gupta, A.K.3    Koshy, A.A.4    Roy, A.5
  • 48
    • 27144498110 scopus 로고    scopus 로고
    • N-linked glycosylation of West Nile virus envelope proteins influences particle assembly and infectivity
    • Hanna SL, Pierson TC, Sanchez MD, Ahmed AA, Murtadha MM, Doms RW: N-linked glycosylation of West Nile virus envelope proteins influences particle assembly and infectivity. J. Virol. 79, 13262-13274 (2005).
    • (2005) J. Virol , vol.79 , pp. 13262-13274
    • Hanna, S.L.1    Pierson, T.C.2    Sanchez, M.D.3    Ahmed, A.A.4    Murtadha, M.M.5    Doms, R.W.6
  • 49
    • 34548605884 scopus 로고    scopus 로고
    • Glycosylation of the Dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes
    • Bryant JE, Calvert AE, Mesesan K et al.: Glycosylation of the Dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes. Virology 366(2), 415-423 (2007).
    • (2007) Virology , vol.366 , Issue.2 , pp. 415-423
    • Bryant, J.E.1    Calvert, A.E.2    Mesesan, K.3
  • 50
    • 17644375905 scopus 로고    scopus 로고
    • Deglycosylation of the NS1 protein of Dengue 2 virus, strain 16681: Construction and characterization of mutant viruses
    • Crabtree MB, Kinney RM, Miller BR: Deglycosylation of the NS1 protein of Dengue 2 virus, strain 16681: construction and characterization of mutant viruses. Arch Virol. 150, 771-786 (2005).
    • (2005) Arch Virol , vol.150 , pp. 771-786
    • Crabtree, M.B.1    Kinney, R.M.2    Miller, B.R.3
  • 51
    • 20744441154 scopus 로고    scopus 로고
    • Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins
    • Goffard A, Callens N, Bartosch B et al.: Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins. J. Virol. 79, 8400-8499 (2005).
    • (2005) J. Virol , vol.79 , pp. 8400-8499
    • Goffard, A.1    Callens, N.2    Bartosch, B.3
  • 52
    • 2942741241 scopus 로고    scopus 로고
    • Influence of N-linked glycans on intracellular transport of hepatitis C virus E1 chimeric glycoprotein and its role in pseudotype virus infectivity
    • Beyene A, Basu A, Meyer K, Ray R: Influence of N-linked glycans on intracellular transport of hepatitis C virus E1 chimeric glycoprotein and its role in pseudotype virus infectivity. Virology 324, 273-285 (2004).
    • (2004) Virology , vol.324 , pp. 273-285
    • Beyene, A.1    Basu, A.2    Meyer, K.3    Ray, R.4
  • 53
    • 0038193898 scopus 로고    scopus 로고
    • Glycosylation of hepatitis C virus envelope proteins
    • Goffard A, Dubuisson J: Glycosylation of hepatitis C virus envelope proteins. Biochimie 85, 295-301 (2003).
    • (2003) Biochimie , vol.85 , pp. 295-301
    • Goffard, A.1    Dubuisson, J.2
  • 54
    • 34547098811 scopus 로고    scopus 로고
    • Hepatitis C virus envelope glycoprotein E2 glycans modulate entry, CD81 binding, and neutralization
    • Falkowska E, Kajumo F, Garcia E, Reinus J, Dragic T: Hepatitis C virus envelope glycoprotein E2 glycans modulate entry, CD81 binding, and neutralization. J. Virol. 81, 8072-8079 (2007).
    • (2007) J. Virol , vol.81 , pp. 8072-8079
    • Falkowska, E.1    Kajumo, F.2    Garcia, E.3    Reinus, J.4    Dragic, T.5
  • 55
    • 19944403933 scopus 로고    scopus 로고
    • Resistance of human immunodeficiency virus type 1 to the high-mannose binding agents cyanovirin N and concanavalin A
    • Witvrouw M, Fikkert V, Hantson A et al.: Resistance of human immunodeficiency virus type 1 to the high-mannose binding agents cyanovirin N and concanavalin A. J. Virol. 79, 7777-7784 (2005).
    • (2005) J. Virol , vol.79 , pp. 7777-7784
    • Witvrouw, M.1    Fikkert, V.2    Hantson, A.3
  • 56
    • 23844475790 scopus 로고    scopus 로고
    • Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man3GlcNAc2: Structural basis for specificity and high-affinity binding to the core pentasaccharide from N-linked oligomannoside
    • Williams DC, Jr., Lee JY, Cai M, Bewley CA, Clore GM: Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man3GlcNAc2: structural basis for specificity and high-affinity binding to the core pentasaccharide from N-linked oligomannoside. J. Biol. Chem. 280, 29269-29276 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 29269-29276
    • Williams Jr., D.C.1    Lee, J.Y.2    Cai, M.3    Bewley, C.A.4    Clore, G.M.5
  • 57
    • 33845897631 scopus 로고    scopus 로고
    • Carbohydrate-binding agents efficiently prevent dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)-directed HIV-1 transmission to T lymphocytes
    • Balzarini J, Van Herrewege Y, Vermeire K, Vanham G, Schols D: Carbohydrate-binding agents efficiently prevent dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)-directed HIV-1 transmission to T lymphocytes. Mol. Pharmacol. 71, 3-11 (2007).
    • (2007) Mol. Pharmacol , vol.71 , pp. 3-11
    • Balzarini, J.1    Van Herrewege, Y.2    Vermeire, K.3    Vanham, G.4    Schols, D.5
  • 58
    • 0043270574 scopus 로고    scopus 로고
    • Potent anti-influenza activity of cyanovirin-N and interactions with viral hemagglutinin
    • O'Keefe BR, Smee DF, Turpin JA et al.: Potent anti-influenza activity of cyanovirin-N and interactions with viral hemagglutinin. Antimicrob. Agents Chemother. 47, 2518-2525 (2003).
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 2518-2525
    • O'Keefe, B.R.1    Smee, D.F.2    Turpin, J.A.3
  • 59
    • 33947275171 scopus 로고    scopus 로고
    • Carbohydrate-binding agents: A potential future cornerstone for the chemotherapy of enveloped viruses?
    • Balzarini J: Carbohydrate-binding agents: a potential future cornerstone for the chemotherapy of enveloped viruses? Antivir. Chem. Chemother. 18, 1-11 (2007).
    • (2007) Antivir. Chem. Chemother , vol.18 , pp. 1-11
    • Balzarini, J.1
  • 60
  • 61
    • 34548150016 scopus 로고    scopus 로고
    • Entry of hepatitis C virus and human immunodeficiency virus is selectively inhibited by carbohydrate-binding agents but not by polyanions
    • Bertaux C, Daelemans D, Meertens L et al.: Entry of hepatitis C virus and human immunodeficiency virus is selectively inhibited by carbohydrate-binding agents but not by polyanions. Virology 366(1), 40-50 (2007).
    • (2007) Virology , vol.366 , Issue.1 , pp. 40-50
    • Bertaux, C.1    Daelemans, D.2    Meertens, L.3
  • 62
    • 34250223426 scopus 로고    scopus 로고
    • Plant lectins are potent inhibitors of coronaviruses by interfering with two targets in the viral replication cycle
    • Keyaerts E, Vijgen L, Pannecouque C et al.: Plant lectins are potent inhibitors of coronaviruses by interfering with two targets in the viral replication cycle. Antiviral Res. 75, 179-187 (2007).
    • (2007) Antiviral Res , vol.75 , pp. 179-187
    • Keyaerts, E.1    Vijgen, L.2    Pannecouque, C.3
  • 63
    • 34447501702 scopus 로고    scopus 로고
    • Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture
    • van der Meer FJ, de Haan CA, Schuurman NM et al.: Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture. Antiviral Res. 76, 21-29 (2007).
    • (2007) Antiviral Res , vol.76 , pp. 21-29
    • van der Meer, F.J.1    de Haan, C.A.2    Schuurman, N.M.3
  • 64
    • 3242876082 scopus 로고    scopus 로고
    • Chloroquine and hydroxydiloroquine as inhibitors of human immunodeficiency virus (HIV-1) activity
    • Romanelli F, Smith KM, Hoven AD: Chloroquine and hydroxydiloroquine as inhibitors of human immunodeficiency virus (HIV-1) activity. Curr. Pharm. Des. 10, 2643-2648 (2004).
    • (2004) Curr. Pharm. Des , vol.10 , pp. 2643-2648
    • Romanelli, F.1    Smith, K.M.2    Hoven, A.D.3
  • 65
    • 0032820180 scopus 로고    scopus 로고
    • Chloroquine exerts an additive in vitro anti-HIV type 1 effect when associated with didanosine and hydroxyurea
    • Boelaert JR, Sperber K, Pierre J: Chloroquine exerts an additive in vitro anti-HIV type 1 effect when associated with didanosine and hydroxyurea. AIDS Res. Hum. Retroviruses 15, 1241-1247 (1999).
    • (1999) AIDS Res. Hum. Retroviruses , vol.15 , pp. 1241-1247
    • Boelaert, J.R.1    Sperber, K.2    Pierre, J.3
  • 66
    • 0029121276 scopus 로고
    • Hydroxychloroquine treatment of patients with human immunodeficiency virus type 1
    • Sperber K, Louie M, Kraus T et al.: Hydroxychloroquine treatment of patients with human immunodeficiency virus type 1. Clin. Ther. 17, 622-636 (1995).
    • (1995) Clin. Ther , vol.17 , pp. 622-636
    • Sperber, K.1    Louie, M.2    Kraus, T.3
  • 67
    • 13944278894 scopus 로고    scopus 로고
    • Hydroxychloroquine, hydroxyurea and didanosine as initial therapy for HIV-infected patients with low viral load: Safety, efficacy and resistance profile after 144 weeks
    • Paton NI, Aboulhab J: Hydroxychloroquine, hydroxyurea and didanosine as initial therapy for HIV-infected patients with low viral load: safety, efficacy and resistance profile after 144 weeks. HIV Med. 6, 13-20 (2005).
    • (2005) HIV Med , vol.6 , pp. 13-20
    • Paton, N.I.1    Aboulhab, J.2
  • 69
    • 25444508979 scopus 로고    scopus 로고
    • Chloroquine is a potent inhibitor of SARS coronavirus infection and spread
    • Vincent MJ, Bergeron E, Benjannet S et al.: Chloroquine is a potent inhibitor of SARS coronavirus infection and spread. Virol. J. 2, 69 (2005).
    • (2005) Virol. J , vol.2 , pp. 69
    • Vincent, M.J.1    Bergeron, E.2    Benjannet, S.3
  • 70
    • 33646166978 scopus 로고    scopus 로고
    • Potential antivirals and antiviral strategies against SARS coronavirus infections
    • De Clercq E: Potential antivirals and antiviral strategies against SARS coronavirus infections. Expert Rev. Anti Infect. Ther. 4, 291-302 (2006).
    • (2006) Expert Rev. Anti Infect. Ther , vol.4 , pp. 291-302
    • De Clercq, E.1
  • 72
    • 34249724532 scopus 로고    scopus 로고
    • Different pH requirements are associated with divergent inhibitory effects of chloroquine on human and avian influenza A viruses
    • Di Trani L, Savarino A, Campitelli L et al.: Different pH requirements are associated with divergent inhibitory effects of chloroquine on human and avian influenza A viruses. Virol. J. 4, 39 (2007).
    • (2007) Virol. J , vol.4 , pp. 39
    • Di Trani, L.1    Savarino, A.2    Campitelli, L.3
  • 73
    • 33745328312 scopus 로고    scopus 로고
    • In vitro inhibition of human influenza A virus replication by chloroquine
    • Ooi EE, Chew JS, Loh JP, Chua RC: In vitro inhibition of human influenza A virus replication by chloroquine. Virol. J. 3, 39 (2006).
    • (2006) Virol. J , vol.3 , pp. 39
    • Ooi, E.E.1    Chew, J.S.2    Loh, J.P.3    Chua, R.C.4
  • 75
    • 34047144973 scopus 로고    scopus 로고
    • Reduction of the infectivity of hepatitis C virus pseudoparticles by incorporation of misfolded glycoproteins induced by glucosidase inhibitors
    • Chapel C, Garcia C, Bartosch B et al.: Reduction of the infectivity of hepatitis C virus pseudoparticles by incorporation of misfolded glycoproteins induced by glucosidase inhibitors. J. Gen. Virol. 88, 1133-1143 (2007).
    • (2007) J. Gen. Virol , vol.88 , pp. 1133-1143
    • Chapel, C.1    Garcia, C.2    Bartosch, B.3
  • 76
    • 33747892601 scopus 로고    scopus 로고
    • Antiviral effects of glycosylation and glucose trimming inhibitors on human parainfluenza virus type 3
    • Tanaka Y, Kato J, Kohara M, Galinski MS: Antiviral effects of glycosylation and glucose trimming inhibitors on human parainfluenza virus type 3. Antiviral Res. 72, 1-9 (2006).
    • (2006) Antiviral Res , vol.72 , pp. 1-9
    • Tanaka, Y.1    Kato, J.2    Kohara, M.3    Galinski, M.S.4
  • 77
    • 0036196402 scopus 로고    scopus 로고
    • Antiviral effects of an iminosugar derivative on flavivirus infections
    • Wu SF, Lee CJ, Liao CL, Dwek RA, Zitzmann N, Lin YL: Antiviral effects of an iminosugar derivative on flavivirus infections. J. Virol. 76, 3596-3604 (2002).
    • (2002) J. Virol , vol.76 , pp. 3596-3604
    • Wu, S.F.1    Lee, C.J.2    Liao, C.L.3    Dwek, R.A.4    Zitzmann, N.5    Lin, Y.L.6
  • 78
    • 34247600576 scopus 로고    scopus 로고
    • The alpha(1,2)-mannosidase I inhibitor 1-deoxymannojirimycin potentiates the antiviral activity of carbohydrate-binding agents against wildtype and mutant HIV-1 strains containing glycan deletions in gp120
    • Balzarini J: The alpha(1,2)-mannosidase I inhibitor 1-deoxymannojirimycin potentiates the antiviral activity of carbohydrate-binding agents against wildtype and mutant HIV-1 strains containing glycan deletions in gp120. FEBS Lett 581, 2060-2064 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 2060-2064
    • Balzarini, J.1
  • 79
    • 0037311412 scopus 로고    scopus 로고
    • Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin
    • Hart ML, Saifuddin M, Spear GT: Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin. G. Gen. Virol. 84, 353-360 (2003).
    • (2003) G. Gen. Virol , vol.84 , pp. 353-360
    • Hart, M.L.1    Saifuddin, M.2    Spear, G.T.3
  • 81
    • 0034577985 scopus 로고    scopus 로고
    • Protein C-mannosylation: Facts and questions
    • Furmanek A, Hofsteenge J: Protein C-mannosylation: facts and questions. Acta Biochim. Pol. 47, 781-789 (2000).
    • (2000) Acta Biochim. Pol , vol.47 , pp. 781-789
    • Furmanek, A.1    Hofsteenge, J.2
  • 82
    • 35348998996 scopus 로고    scopus 로고
    • Ebola sGP-the first viral glycoprotein shown to be C-mannosylated
    • Epub ahead of print
    • Falzarano D, Krokhin O, Van Domselaar G et al.: Ebola sGP-the first viral glycoprotein shown to be C-mannosylated. Virology (Epub ahead of print) (2007).
    • (2007) Virology
    • Falzarano, D.1    Krokhin, O.2    Van Domselaar, G.3
  • 83
    • 0347122962 scopus 로고    scopus 로고
    • Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
    • Cambi A, de Lange F, van Maarseveen NM et al.: Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells. J. Cell Biol. 164, 145-155 (2004).
    • (2004) J. Cell Biol , vol.164 , pp. 145-155
    • Cambi, A.1    de Lange, F.2    van Maarseveen, N.M.3
  • 84
    • 0141533076 scopus 로고    scopus 로고
    • Dual function of C-type lectin-like receptors in the immune system
    • Cambi A, Figdor CG: Dual function of C-type lectin-like receptors in the immune system. Curr. Opin. Cell Biol. 15, 539-546 (2003).
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 539-546
    • Cambi, A.1    Figdor, C.G.2
  • 85
    • 0034063448 scopus 로고    scopus 로고
    • Involvement of the mannose receptor in infection of macrophages by influenza virus
    • Reading PC, Miller JL, Anders EM: Involvement of the mannose receptor in infection of macrophages by influenza virus. J. Virol. 74, 5190-5197 (2000).
    • (2000) J. Virol , vol.74 , pp. 5190-5197
    • Reading, P.C.1    Miller, J.L.2    Anders, E.M.3
  • 86
    • 0037331514 scopus 로고    scopus 로고
    • Involvement of macrophage mannose receptor in the binding and transmission of HIV by macrophages
    • Nguyen DG, Hildreth JE: Involvement of macrophage mannose receptor in the binding and transmission of HIV by macrophages. Eur. J. Immunol. 33, 483-493 (2003).
    • (2003) Eur. J. Immunol , vol.33 , pp. 483-493
    • Nguyen, D.G.1    Hildreth, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.