메뉴 건너뛰기




Volumn 30, Issue 5, 1998, Pages 435-440

Host cell glycosylation of viral glycoproteins - A battlefield for host defence and viral resistance

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; GLYCAN; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 0032444735     PISSN: 00365548     EISSN: None     Source Type: Journal    
DOI: 10.1080/00365549850161386     Document Type: Review
Times cited : (59)

References (39)
  • 1
    • 0029927634 scopus 로고    scopus 로고
    • Early region 3 (E3) of adenovirus type 19 (subgroup D) encodes an HLA-binding protein distinct from that of subgroups B and C
    • Deryckere F, Burgert HG. Early region 3 (E3) of adenovirus type 19 (subgroup D) encodes an HLA-binding protein distinct from that of subgroups B and C. J Virol 1996; 70: 2832-41.
    • (1996) J Virol , vol.70 , pp. 2832-2841
    • Deryckere, F.1    Burgert, H.G.2
  • 2
    • 0029887717 scopus 로고    scopus 로고
    • Human herpes simplex virus (HSV)-specific CD8 + CTL clones recognize HSV-2-infected fibroblasts after treatment with IFN-gamma or when virion host shutoff functions are disabled
    • Tiggs MA, Leng S, Johnson DC, Burke RL. Human herpes simplex virus (HSV)-specific CD8 + CTL clones recognize HSV-2-infected fibroblasts after treatment with IFN-gamma or when virion host shutoff functions are disabled. J Immunol 1996; 156: 3901-10.
    • (1996) J Immunol , vol.156 , pp. 3901-3910
    • Tiggs, M.A.1    Leng, S.2    Johnson, D.C.3    Burke, R.L.4
  • 3
    • 0023618761 scopus 로고
    • Inhibitors of protein glycosylation and glycoprotein processing in viral systems
    • Datema R, Olofsson S, Romero P. Inhibitors of protein glycosylation and glycoprotein processing in viral systems. Pharmac Ther 1987; 33: 221-86.
    • (1987) Pharmac Ther , vol.33 , pp. 221-286
    • Datema, R.1    Olofsson, S.2    Romero, P.3
  • 4
    • 15844386264 scopus 로고
    • Complex carbohydrates and intercellular adhesion
    • Lee EYC, Smith EE, eds. New York: Academic Press
    • Roseman S. Complex carbohydrates and intercellular adhesion. In: Lee EYC, Smith EE, eds. Biology and chemistry of eucaryotic cell surfaces. New York: Academic Press 1974: 317-54.
    • (1974) Biology and Chemistry of Eucaryotic Cell Surfaces , pp. 317-354
    • Roseman, S.1
  • 5
    • 0014220156 scopus 로고
    • Mechanism of epsilon-15 conversion studied with a bacterial mutant
    • Losick R, Robbins PW. Mechanism of epsilon-15 conversion studied with a bacterial mutant. J Mol Biol 1967; 30: 445-55.
    • (1967) J Mol Biol , vol.30 , pp. 445-455
    • Losick, R.1    Robbins, P.W.2
  • 6
    • 0024965003 scopus 로고
    • A baculovirus blocks insect molting by producing ecdysteroid UDP-glucosyl transferase
    • O'Reilly DR, Miller RK. A baculovirus blocks insect molting by producing ecdysteroid UDP-glucosyl transferase. Science 1989; 245: 1110-2.
    • (1989) Science , vol.245 , pp. 1110-1112
    • O'Reilly, D.R.1    Miller, R.K.2
  • 7
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 1988; 332: 462-4.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 8
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley SM, Bole DG, Hoover-Litty H, Helenius A, Copeland CS. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J Cell Biol 1989; 108: 2117-26.
    • (1989) J Cell Biol , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 9
    • 0026458851 scopus 로고
    • Carbohydrates of human immunodeficiency virus
    • Hansen JE. Carbohydrates of human immunodeficiency virus. APMIS 1992; Suppl 27: 96-108.
    • (1992) APMIS , Issue.27 SUPPL. , pp. 96-108
    • Hansen, J.E.1
  • 10
    • 0026451772 scopus 로고
    • Carbohydrates in herpesvirus infections
    • Olofsson S. Carbohydrates in herpesvirus infections. APMIS 1992; 100: 84-95.
    • (1992) APMIS , vol.100 , pp. 84-95
    • Olofsson, S.1
  • 12
    • 0026642422 scopus 로고
    • Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size
    • Munk K, Pritzer E, Kretzschmar E, Gutte B, Garten W, Klenk HD. Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size. Glycobiology 1992; 2: 233-40.
    • (1992) Glycobiology , vol.2 , pp. 233-240
    • Munk, K.1    Pritzer, E.2    Kretzschmar, E.3    Gutte, B.4    Garten, W.5    Klenk, H.D.6
  • 13
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 1990; 265: 10373-82.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 14
    • 0023811767 scopus 로고
    • Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein gp120
    • Geyer H, Holschbach C, Hunsmann G. Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein gp120. J Biol Chem 1988; 263: 11760-7.
    • (1988) J Biol Chem , vol.263 , pp. 11760-11767
    • Geyer, H.1    Holschbach, C.2    Hunsmann, G.3
  • 15
    • 0027531918 scopus 로고
    • Pathogenesis of human immunideficiency virus
    • Levy JA. Pathogenesis of human immunideficiency virus. Microbiolog Rev 1993; 57: 183-289.
    • (1993) Microbiolog Rev , vol.57 , pp. 183-289
    • Levy, J.A.1
  • 16
    • 0029940696 scopus 로고    scopus 로고
    • Rapid selection of an N-linked oligosaccharide by monoclonal antibodies against the V3-loop of HIV-1
    • Schønning K, Jansson B, Olofsson S, Hansen J-ES. Rapid selection of an N-linked oligosaccharide by monoclonal antibodies against the V3-loop of HIV-1. J Gen Virol 1996; 77: 753-8.
    • (1996) J Gen Virol , vol.77 , pp. 753-758
    • Schønning, K.1    Jansson, B.2    Olofsson, S.3    Hansen, J.-E.S.4
  • 17
    • 0029912187 scopus 로고    scopus 로고
    • Resistance to V3-directed neutralization caused by an N-linked oligosaccharide depends on the quartenary structure of the HIV-1 envelope oligomer
    • Schønning K, Jansson B, Olofsson S, Nielsen JO, Hansen J-ES. Resistance to V3-directed neutralization caused by an N-linked oligosaccharide depends on the quartenary structure of the HIV-1 envelope oligomer. Virology 1996; 218: 134-40.
    • (1996) Virology , vol.218 , pp. 134-140
    • Schønning, K.1    Jansson, B.2    Olofsson, S.3    Nielsen, J.O.4    Hansen, J.-E.S.5
  • 19
    • 33646282720 scopus 로고    scopus 로고
    • Myers G, Korber B, Berzofsky JA, Smith RF, Pavlakis GN. Los Alamos. Los Alamos National Laboratory, 1992
    • Myers G, Korber B, Berzofsky JA, Smith RF, Pavlakis GN. Los Alamos. Los Alamos National Laboratory, 1992.
  • 20
    • 0026760891 scopus 로고
    • Carbohydrates of the cell surface: Molecular aspects of glycosyl transferases and their genes
    • Clausen H, Bennett EP, Dabelsteen E. Carbohydrates of the cell surface: molecular aspects of glycosyl transferases and their genes. APMIS 1992; 100: 9-17.
    • (1992) APMIS , vol.100 , pp. 9-17
    • Clausen, H.1    Bennett, E.P.2    Dabelsteen, E.3
  • 21
    • 0023819030 scopus 로고
    • Expression of Ley antigen in human immunodeficiency virus-infected human T-cell lines and in peripheral lymphocytes of patients with acquired immune deficiency syndrome (AIDS) and AIDS-related complex
    • Adachi M, Hayami M, Kashiwagi N, Mizuta T, Ohta Gill MJ, Matheson DS, Tamaoki T, Shiozawa C, Hakomori S-I. Expression of Ley antigen in human immunodeficiency virus-infected human T-cell lines and in peripheral lymphocytes of patients with acquired immune deficiency syndrome (AIDS) and AIDS-related complex. J Exp Med 1988; 167: 323-31.
    • (1988) J Exp Med , vol.167 , pp. 323-331
    • Adachi, M.1    Hayami, M.2    Kashiwagi, N.3    Mizuta, T.4    Ohta Gill, M.J.5    Matheson, D.S.6    Tamaoki, T.7    Shiozawa, C.8    Hakomori, S.-I.9
  • 22
    • 0025315127 scopus 로고
    • Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: Peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization
    • Hansen JE, Clausen H, Nielsen C, Teglbjaerg LS, Hansen LL, Nielsen CM, Dabelsteen E, Mathiesen L, Hakomori SI, Nielsen JO. Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization. J Virol 1990; 64: 2833-40.
    • (1990) J Virol , vol.64 , pp. 2833-2840
    • Hansen, J.E.1    Clausen, H.2    Nielsen, C.3    Teglbjaerg, L.S.4    Hansen, L.L.5    Nielsen, C.M.6    Dabelsteen, E.7    Mathiesen, L.8    Hakomori, S.I.9    Nielsen, J.O.10
  • 24
    • 0028267244 scopus 로고
    • Selective suppression of N-acetylglucosaminyltransferase III activity in a human hepatoblastoma cell line transfected with hepatitis B virus
    • Miyoshi E, Nishikawa A, Ihara Y, Hayashi N, Fusamoto H, Kamada T, Taniguchi N. Selective suppression of N-acetylglucosaminyltransferase III activity in a human hepatoblastoma cell line transfected with hepatitis B virus. Cancer Res 1994; 54: 1854-8.
    • (1994) Cancer Res , vol.54 , pp. 1854-1858
    • Miyoshi, E.1    Nishikawa, A.2    Ihara, Y.3    Hayashi, N.4    Fusamoto, H.5    Kamada, T.6    Taniguchi, N.7
  • 25
    • 0019510274 scopus 로고
    • Heterophil antibodies recognize oncovirus envelope antigens: Epidemiological parameters and immunological specificity of the reaction
    • Löwer J, Davidson E, Teich NM, Weiss RA, Joseph AP, Kurth R. Heterophil antibodies recognize oncovirus envelope antigens: epidemiological parameters and immunological specificity of the reaction. Virology 1981; 109: 409-17.
    • (1981) Virology , vol.109 , pp. 409-417
    • Löwer, J.1    Davidson, E.2    Teich, N.M.3    Weiss, R.A.4    Joseph, A.P.5    Kurth, R.6
  • 26
    • 9244228605 scopus 로고
    • Influence of glycosylation on antigenicity of viral proteins
    • van Regenmortel MHV, Neurath AR, eds. Amsterdam: Elsevier
    • Klenk H-D. Influence of glycosylation on antigenicity of viral proteins. In: van Regenmortel MHV, Neurath AR, eds. The basis for serodiagnosis and vaccins. Amsterdam: Elsevier, 1990: 25-37.
    • (1990) The Basis for Serodiagnosis and Vaccins , pp. 25-37
    • Klenk, H.-D.1
  • 27
    • 0016215743 scopus 로고
    • Influnece of orally administered antibiotocs on anti-T agglutinin of normal subjects and of cirrhotic patients
    • Boccardi V, Attina D, Girelli G. Influnece of orally administered antibiotocs on anti-T agglutinin of normal subjects and of cirrhotic patients. Vox sanguinis 1974; 27: 268-72.
    • (1974) Vox Sanguinis , vol.27 , pp. 268-272
    • Boccardi, V.1    Attina, D.2    Girelli, G.3
  • 29
    • 0025773203 scopus 로고
    • Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys
    • Galili U, Swanson K. Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc Natl Acad Sci USA 1991; 88: 7401-4.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7401-7404
    • Galili, U.1    Swanson, K.2
  • 31
    • 0023950850 scopus 로고
    • Interaction between human natural anti-alpha-galactosyl immunoglobulin G and bacteria of the human flora
    • Galili U, Mandrell RE, Hamadeh RM, Shohet SB, Griffiss JM. Interaction between human natural anti-alpha-galactosyl immunoglobulin G and bacteria of the human flora. Infect Immun 1988; 56: 1730-7.
    • (1988) Infect Immun , vol.56 , pp. 1730-1737
    • Galili, U.1    Mandrell, R.E.2    Hamadeh, R.M.3    Shohet, S.B.4    Griffiss, J.M.5
  • 32
    • 0028268967 scopus 로고
    • Differential host dependent expression of alpha-galactosyl epitopes on viral glycoproteins: A study of eastern equine encephalitis virus as a model
    • Repik PM, Strizki JM, Galili U. Differential host dependent expression of alpha-galactosyl epitopes on viral glycoproteins: a study of eastern equine encephalitis virus as a model. J Gen Virol 1994; 75: 1177-81.
    • (1994) J Gen Virol , vol.75 , pp. 1177-1181
    • Repik, P.M.1    Strizki, J.M.2    Galili, U.3
  • 34
    • 0031054438 scopus 로고    scopus 로고
    • Infection of human cells by an endogenous retrovirus of pigs
    • Patience C, Takeuchi Y, Weiss RA. Infection of human cells by an endogenous retrovirus of pigs. Nat Med 1997; 3: 282-6.
    • (1997) Nat Med , vol.3 , pp. 282-286
    • Patience, C.1    Takeuchi, Y.2    Weiss, R.A.3
  • 35
    • 0032556895 scopus 로고    scopus 로고
    • Transgenic pigs and virus adaption
    • Weiss R. Transgenic pigs and virus adaption. Nature 1998; 391: 327-8.
    • (1998) Nature , vol.391 , pp. 327-328
    • Weiss, R.1
  • 38
    • 0002971277 scopus 로고
    • Use of lectins in general and diagnostic virology
    • Doyle, RJ, Slifkin, M, eds. New York: Marcel Dekker Inc
    • Olofsson S, Jeansson S, Hansen J-ES. Use of lectins in general and diagnostic virology. In: Doyle, RJ, Slifkin, M, eds. Lectin-microrganism interactions. New York: Marcel Dekker Inc, 1994:67-109.
    • (1994) Lectin-microrganism Interactions , pp. 67-109
    • Olofsson, S.1    Jeansson, S.2    Hansen, J.-E.S.3
  • 39
    • 0025810574 scopus 로고
    • Antibody to histo-blood group a antigen neutralizes HIV produced by lymphocytes from blood group a donors but not from blood group B or O donors
    • Arendup M, Hansen JE, Clausen H, Nielsen C, Mathiesen LR, Nielson JO. Antibody to histo-blood group A antigen neutralizes HIV produced by lymphocytes from blood group A donors but not from blood group B or O donors. AIDS 1991; 5: 441-4.
    • (1991) AIDS , vol.5 , pp. 441-444
    • Arendup, M.1    Hansen, J.E.2    Clausen, H.3    Nielsen, C.4    Mathiesen, L.R.5    Nielson, J.O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.