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Volumn 88, Issue 6, 2007, Pages 1683-1688

Glycoprotein I of herpes simplex virus type 1 contains a unique polymorphic tandem-repeated mucin region

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN I; MUCIN; N ACETYLGALACTOSAMINYLTRANSFERASE; N ACETYLGALACTOSAMINYLTRANSFERASE T1; N ACETYLGALACTOSAMINYLTRANSFERASE T11; N ACETYLGALACTOSAMINYLTRANSFERASE T2; N ACETYLGALACTOSAMINYLTRANSFERASE T3; N ACETYLGALACTOSAMINYLTRANSFERASE T4; SERINE; THREONINE; TN ANTIGEN; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

EID: 34249774865     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.82500-0     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 0030636948 scopus 로고    scopus 로고
    • Mapping regions of herpes simplex virus type 1 glycoprotein I required for formation of the viral Fc receptor for monomeric IgG
    • Basu, S., Dubin, G., Nagashunmugam, T., Basu, M., Goldstein, L. T., Wang, L., Weeks, B. & Friedman, H. M. (1997). Mapping regions of herpes simplex virus type 1 glycoprotein I required for formation of the viral Fc receptor for monomeric IgG. J Immunol 158, 209-215.
    • (1997) J Immunol , vol.158 , pp. 209-215
    • Basu, S.1    Dubin, G.2    Nagashunmugam, T.3    Basu, M.4    Goldstein, L.T.5    Wang, L.6    Weeks, B.7    Friedman, H.M.8
  • 2
    • 15444344929 scopus 로고    scopus 로고
    • Cloning of a human UDP-N-acetyl-α-D-galactosamine: Polypeptide N-acetylgalactosaminyl-transferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat
    • Bennett, E. P., Hassan, H., Mandel, U., Mirgorodskaya, E., Roepstorff, P., Burchell, J., Taylor-Papadimitriou, J., Hollingsworth, M. A., Merkx, G. & other authors (1998). Cloning of a human UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyl-transferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. J Biol Chem 273, 30472-30481.
    • (1998) J Biol Chem , vol.273 , pp. 30472-30481
    • Bennett, E.P.1    Hassan, H.2    Mandel, U.3    Mirgorodskaya, E.4    Roepstorff, P.5    Burchell, J.6    Taylor-Papadimitriou, J.7    Hollingsworth, M.A.8    Merkx, G.9
  • 3
    • 0033520457 scopus 로고    scopus 로고
    • Cloning and characterization of a close homologue of human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy
    • Bennett, E. P., Hassan, H., Mandel, U., Hollingsworth, M. A., Akisawa, N., Ikematsu, Y., Merkx, G., van Kassel, A. G., Olofsson, S. & Clausen, H. (1999). Cloning and characterization of a close homologue of human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J Biol Chem 274, 25362-25370.
    • (1999) J Biol Chem , vol.274 , pp. 25362-25370
    • Bennett, E.P.1    Hassan, H.2    Mandel, U.3    Hollingsworth, M.A.4    Akisawa, N.5    Ikematsu, Y.6    Merkx, G.7    van Kassel, A.G.8    Olofsson, S.9    Clausen, H.10
  • 4
    • 0033548620 scopus 로고    scopus 로고
    • Characterization of the interaction between the herpes simplex virus type I Fc receptor and immunoglobulin G
    • Chapman, T. L., You, L, Joseph, I. M., Bjorkman, P. J., Morrison, S. L. & Raghavan, M. (1999). Characterization of the interaction between the herpes simplex virus type I Fc receptor and immunoglobulin G. J Biol Chem 274, 6911-6919.
    • (1999) J Biol Chem , vol.274 , pp. 6911-6919
    • Chapman, T.L.1    You, L.2    Joseph, I.M.3    Bjorkman, P.J.4    Morrison, S.L.5    Raghavan, M.6
  • 5
    • 0029854393 scopus 로고    scopus 로고
    • A family of UDP-GalNAc: Polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation
    • Clausen, H. & Bennett, E. P. (1996). A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation. Glycobiology 6, 635-646.
    • (1996) Glycobiology , vol.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 7
    • 0031690758 scopus 로고    scopus 로고
    • The herpes simplex virus gE-gl complex facilitates cell-to-cell spread and binds to components of cell junctions
    • Dingwell, K. S. & Johnson, D. C. (1998). The herpes simplex virus gE-gl complex facilitates cell-to-cell spread and binds to components of cell junctions. J Virol 72, 8933-8942.
    • (1998) J Virol , vol.72 , pp. 8933-8942
    • Dingwell, K.S.1    Johnson, D.C.2
  • 8
    • 0028849767 scopus 로고
    • Glycoproteins E and I facilitate neuron-to-neuron spread of herpes simplex virus
    • Dingwall, K. S., Doering, L. C. & Johnson, D. C. (1995). Glycoproteins E and I facilitate neuron-to-neuron spread of herpes simplex virus. J Virol 69, 7087-7098.
    • (1995) J Virol , vol.69 , pp. 7087-7098
    • Dingwall, K.S.1    Doering, L.C.2    Johnson, D.C.3
  • 9
    • 0025302970 scopus 로고
    • Herpes simplex virus type 1 encodes two Fc receptors which have different binding characteristics for monomeric immunoglobulin G (IgG) and IgG complexes
    • Dubin, G., Frank, I. & Friedman, H. M. (1990). Herpes simplex virus type 1 encodes two Fc receptors which have different binding characteristics for monomeric immunoglobulin G (IgG) and IgG complexes. J Virol 64, 2725-2731.
    • (1990) J Virol , vol.64 , pp. 2725-2731
    • Dubin, G.1    Frank, I.2    Friedman, H.M.3
  • 10
    • 0017832443 scopus 로고
    • The lectins: Carbohydrate-binding proteins of plants and animals
    • Goldstein, I. J. & Hayes, C. E. (1978). The lectins: carbohydrate-binding proteins of plants and animals. Adv Carbohydr Chem Biochem 35, 127-340.
    • (1978) Adv Carbohydr Chem Biochem , vol.35 , pp. 127-340
    • Goldstein, I.J.1    Hayes, C.E.2
  • 11
    • 0028107095 scopus 로고
    • Towards characterizing O-glycans: The relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites
    • Gooley, A. A. & Williams, K. L. (1994). Towards characterizing O-glycans: the relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites. Glycobiology 4, 413-417.
    • (1994) Glycobiology , vol.4 , pp. 413-417
    • Gooley, A.A.1    Williams, K.L.2
  • 12
    • 0027965212 scopus 로고
    • The herpes simplex virus type 1 particle: Structure and molecular functionsReview article.)
    • Haarr, L. & Skulstad, S. (1994). The herpes simplex virus type 1 particle: structure and molecular functionsReview article.). APMIS 102, 321-346.
    • (1994) APMIS , vol.102 , pp. 321-346
    • Haarr, L.1    Skulstad, S.2
  • 13
    • 0025280274 scopus 로고
    • Herpes simplex virus IgG Fc receptors induced using recombinant adenovirus vectors expressing glycoproteins E and I
    • Hanke, T., Graham, F. L., Lulitanond, V. & Johnson, D. C. (1990). Herpes simplex virus IgG Fc receptors induced using recombinant adenovirus vectors expressing glycoproteins E and I. Virology 177, 437-444.
    • (1990) Virology , vol.177 , pp. 437-444
    • Hanke, T.1    Graham, F.L.2    Lulitanond, V.3    Johnson, D.C.4
  • 14
    • 0010200397 scopus 로고    scopus 로고
    • O-glycan occupancy is directed by substrate specificities of polypeptide GalNAc-transferases
    • Edited by B. Ernst, B. W. Hart & P. Sina. New York: Wiley-VCH
    • Hassan, H., Bennett, E. P., Mandel, U., Hollingsworth, M. A. & Clausen, H. (2000). O-glycan occupancy is directed by substrate specificities of polypeptide GalNAc-transferases. In Carbohydrates in Chemistry and Biology, pp. 271-292. Edited by B. Ernst, B. W. Hart & P. Sina. New York: Wiley-VCH.
    • (2000) Carbohydrates in Chemistry and Biology , pp. 271-292
    • Hassan, H.1    Bennett, E.P.2    Mandel, U.3    Hollingsworth, M.A.4    Clausen, H.5
  • 15
    • 0025297888 scopus 로고
    • Why are proteins O-glycosylated?
    • Jentoft, N. (1990). Why are proteins O-glycosylated? Trends Biochem Sci 15, 291-294.
    • (1990) Trends Biochem Sci , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 16
    • 0023252169 scopus 로고
    • Identification of a novel herpes simplex virus type 1-induced glycoprotein which complexes with gE and binds immunoglobulin
    • Johnson, D. C. & Feenstra, V, (1987). Identification of a novel herpes simplex virus type 1-induced glycoprotein which complexes with gE and binds immunoglobulin. J Virol 61, 2208-2216.
    • (1987) J Virol , vol.61 , pp. 2208-2216
    • Johnson, D.C.1    Feenstra, V.2
  • 17
    • 0023834392 scopus 로고
    • Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI
    • Johnson, D. C., Frame, M. C., Ligas, M. W., Cross, A. M. & Stow, N. D. (1988). Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI. J Virol 62, 1347-1354.
    • (1988) J Virol , vol.62 , pp. 1347-1354
    • Johnson, D.C.1    Frame, M.C.2    Ligas, M.W.3    Cross, A.M.4    Stow, N.D.5
  • 18
    • 0033934910 scopus 로고    scopus 로고
    • First episodes of genital herpes in a Swedish STD population: A study of epidemiology and transmission by the use of herpes simplex virus (FISV) typing and specific serology
    • Löwhagen, G.-B., Tunbäck, P., Andersson, K., Bergström, T. & Johannisson, G. (2000). First episodes of genital herpes in a Swedish STD population: a study of epidemiology and transmission by the use of herpes simplex virus (FISV) typing and specific serology. Sex Transm Infect 76, 179-182.
    • (2000) Sex Transm Infect , vol.76 , pp. 179-182
    • Löwhagen, G.-B.1    Tunbäck, P.2    Andersson, K.3    Bergström, T.4    Johannisson, G.5
  • 19
    • 0023462539 scopus 로고
    • Host cell-induced differences in O-glycosylation of herpes simplex virus gC-1
    • Lundström, M., Olofsson, S., Jeansson, S., Lycke, E., Datema, R. & Månsson, J. (1987). Host cell-induced differences in O-glycosylation of herpes simplex virus gC-1. Virology 161, 385-394.
    • (1987) Virology , vol.161 , pp. 385-394
    • Lundström, M.1    Olofsson, S.2    Jeansson, S.3    Lycke, E.4    Datema, R.5    Månsson, J.6
  • 21
    • 0032939863 scopus 로고    scopus 로고
    • Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: Immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family
    • Mandel, U., Hassan, H., Therkildsen, M. H., Rygaard, J., Jakobsen, M. H., Juhl, B. R., Dabelsteen, E. & Clausen, H. (1999). Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. Glycobiology 9, 43-52.
    • (1999) Glycobiology , vol.9 , pp. 43-52
    • Mandel, U.1    Hassan, H.2    Therkildsen, M.H.3    Rygaard, J.4    Jakobsen, M.H.5    Juhl, B.R.6    Dabelsteen, E.7    Clausen, H.8
  • 22
    • 0022354892 scopus 로고
    • Sequence determination and genetic content of the short unique region in the genome of herpes simplex virus type 1
    • McGeoch, D. J., Dolan, A., Donald, S. & Rixon, F. J. (1985). Sequence determination and genetic content of the short unique region in the genome of herpes simplex virus type 1. J Mol Biol 181, 1-13.
    • (1985) J Mol Biol , vol.181 , pp. 1-13
    • McGeoch, D.J.1    Dolan, A.2    Donald, S.3    Rixon, F.J.4
  • 23
    • 0023056480 scopus 로고
    • Complete DNA sequence of the short repeat region in the genome of herpes simplex virus type 1
    • McGeoch, D. J., Dolan, A., Donald, S. & Brauer, D. H. (1986). Complete DNA sequence of the short repeat region in the genome of herpes simplex virus type 1. Nucleic Acids Res 14, 1727-1745.
    • (1986) Nucleic Acids Res , vol.14 , pp. 1727-1745
    • McGeoch, D.J.1    Dolan, A.2    Donald, S.3    Brauer, D.H.4
  • 25
    • 4644259016 scopus 로고    scopus 로고
    • Phylogenetic analysis of clinical herpes simplex virus type 1 isolates identified three genetic groups and recombinant viruses
    • Norberg, P., Bergström, T., Rekabdar, E., Lindh, M. & Liljeqvist, J.-A. (2004). Phylogenetic analysis of clinical herpes simplex virus type 1 isolates identified three genetic groups and recombinant viruses. J Virol 78, 10755-10764.
    • (2004) J Virol , vol.78 , pp. 10755-10764
    • Norberg, P.1    Bergström, T.2    Rekabdar, E.3    Lindh, M.4    Liljeqvist, J.-A.5
  • 26
    • 0026451772 scopus 로고
    • Carbohydrates in herpesvirus infections
    • Olofsson, S. (1992). Carbohydrates in herpesvirus infections. APMIS 100, 84-95.
    • (1992) APMIS , vol.100 , pp. 84-95
    • Olofsson, S.1
  • 27
    • 0023709407 scopus 로고
    • The DNA sequences of the long repeat region and adjoining parts of the long unique region in the genome of herpes simplex virus type 1
    • Perry, L. J. & McGeoch, D. J. (1988). The DNA sequences of the long repeat region and adjoining parts of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol 69, 2831-2846.
    • (1988) J Gen Virol , vol.69 , pp. 2831-2846
    • Perry, L.J.1    McGeoch, D.J.2
  • 28
    • 33747883766 scopus 로고    scopus 로고
    • Cell surface-associated mucins in signal transduction
    • Singh, P. K. & Hollingsworth, M. A. (2006). Cell surface-associated mucins in signal transduction. Trends Cell Biol 16, 467-476.
    • (2006) Trends Cell Biol , vol.16 , pp. 467-476
    • Singh, P.K.1    Hollingsworth, M.A.2
  • 29
    • 0026539530 scopus 로고
    • Antigenic structure of the herpes simplex virus type 1 glycoprotein C: Demonstration of a linear epitope situated in an environment of highly conformation-dependent epitopes
    • Sjoblom, I., Glorioso, J. C., Sjogren-Jansson, E. & Olofsson, S. (1992). Antigenic structure of the herpes simplex virus type 1 glycoprotein C: demonstration of a linear epitope situated in an environment of highly conformation-dependent epitopes. APMIS 100, 229-236.
    • (1992) APMIS , vol.100 , pp. 229-236
    • Sjoblom, I.1    Glorioso, J.C.2    Sjogren-Jansson, E.3    Olofsson, S.4
  • 30
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases
    • Ten Hagen, K. G., Fritz, T. A. & Tabak, L. A. (2003). All in the family: the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13, 1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 32
    • 0030798627 scopus 로고    scopus 로고
    • Substrate specificities of three members of the human UDP-N-acetyl-α-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-TI, -T2, and -T3
    • Wandall, H. H., Hassan, H., Mirgorodskaya, E., Kristensen, A. K., Roepstorff, P., Bennett, E. P., Nielsen, P. A., Hollingsworth, M. A., Burchell, J. & other authors (1997). Substrate specificities of three members of the human UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase family, GalNAc-TI, -T2, and -T3. J Biol Chem 272, 23503-23514.
    • (1997) J Biol Chem , vol.272 , pp. 23503-23514
    • Wandall, H.H.1    Hassan, H.2    Mirgorodskaya, E.3    Kristensen, A.K.4    Roepstorff, P.5    Bennett, E.P.6    Nielsen, P.A.7    Hollingsworth, M.A.8    Burchell, J.9


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