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Volumn 388, Issue 2, 2009, Pages 335-343

EBV BMRF-2 facilitates cell-to-cell spread of virus within polarized oral epithelial cells

Author keywords

EBV BMRF 2; EBV cell to cell spread

Indexed keywords

BMRF 2 PROTEIN; LEUCINE; MEMBRANE PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 67349183927     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.03.030     Document Type: Article
Times cited : (41)

References (66)
  • 2
    • 0029858530 scopus 로고    scopus 로고
    • A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network
    • Alconada A., Bauer U., and Hoflack B. A tyrosine-based motif and a casein kinase II phosphorylation site regulate the intracellular trafficking of the varicella-zoster virus glycoprotein I, a protein localized in the trans-Golgi network. EMBO J. 15 22 (1996) 6096-6110
    • (1996) EMBO J. , vol.15 , Issue.22 , pp. 6096-6110
    • Alconada, A.1    Bauer, U.2    Hoflack, B.3
  • 3
    • 0032577479 scopus 로고    scopus 로고
    • Intracellular transport of the glycoproteins gE and gI of the varicella-zoster virus. gE accelerates the maturation of gI and determines its accumulation in the trans-Golgi network
    • Alconada A., Bauer U., Baudoux L., Piette J., and Hoflack B. Intracellular transport of the glycoproteins gE and gI of the varicella-zoster virus. gE accelerates the maturation of gI and determines its accumulation in the trans-Golgi network. J. Biol. Chem. 273 22 (1998) 13430-13436
    • (1998) J. Biol. Chem. , vol.273 , Issue.22 , pp. 13430-13436
    • Alconada, A.1    Bauer, U.2    Baudoux, L.3    Piette, J.4    Hoflack, B.5
  • 4
    • 0032889509 scopus 로고    scopus 로고
    • Intracellular traffic of herpes simplex virus glycoprotein gE: characterization of the sorting signals required for its trans-Golgi network localization
    • Alconada A., Bauler U., Sodiek B., and Hoflack B. Intracellular traffic of herpes simplex virus glycoprotein gE: characterization of the sorting signals required for its trans-Golgi network localization. J. Virol. 73 (1998) 377-387
    • (1998) J. Virol. , vol.73 , pp. 377-387
    • Alconada, A.1    Bauler, U.2    Sodiek, B.3    Hoflack, B.4
  • 5
    • 0028229074 scopus 로고
    • An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ
    • Balan P., Davis P.N., Bell S., Atkinson H., Browne H., and Minson T. An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ. J. Gen. Virol. 75 Pt 6 (1994) 1245-1258
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART 6 , pp. 1245-1258
    • Balan, P.1    Davis, P.N.2    Bell, S.3    Atkinson, H.4    Browne, H.5    Minson, T.6
  • 6
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 7
    • 0030179367 scopus 로고    scopus 로고
    • Mechanisms of signal-mediated protein sorting in the endocytic and secretory pathways
    • Bonifacino J.S., Marks M.S., Ohno H., and Kirchhausen T. Mechanisms of signal-mediated protein sorting in the endocytic and secretory pathways. Proc. Assoc. Am. Physicians 108 4 (1996) 285-295
    • (1996) Proc. Assoc. Am. Physicians , vol.108 , Issue.4 , pp. 285-295
    • Bonifacino, J.S.1    Marks, M.S.2    Ohno, H.3    Kirchhausen, T.4
  • 8
    • 0033995281 scopus 로고    scopus 로고
    • Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation
    • Brack A.R., Klupp B.G., Granzow H., Tirabassi R., Enquist L.W., and Mettenleiter T.C. Role of the cytoplasmic tail of pseudorabies virus glycoprotein E in virion formation. J. Virol. 74 9 (2000) 4004-4016
    • (2000) J. Virol. , vol.74 , Issue.9 , pp. 4004-4016
    • Brack, A.R.1    Klupp, B.G.2    Granzow, H.3    Tirabassi, R.4    Enquist, L.W.5    Mettenleiter, T.C.6
  • 9
    • 0029949793 scopus 로고    scopus 로고
    • An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress
    • Browne H., Bell S., Minson T., and Wilson D.W. An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress. J. Virol. 70 7 (1996) 4311-4316
    • (1996) J. Virol. , vol.70 , Issue.7 , pp. 4311-4316
    • Browne, H.1    Bell, S.2    Minson, T.3    Wilson, D.W.4
  • 10
    • 0032824654 scopus 로고    scopus 로고
    • Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes
    • Chang Y., Tung C.H., Huang Y.T., Lu J., Chen J.Y., and Tsai C.H. Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes. J. Virol. 73 10 (1999) 8857-8866
    • (1999) J. Virol. , vol.73 , Issue.10 , pp. 8857-8866
    • Chang, Y.1    Tung, C.H.2    Huang, Y.T.3    Lu, J.4    Chen, J.Y.5    Tsai, C.H.6
  • 11
    • 0033548575 scopus 로고    scopus 로고
    • AP-4, a novel protein complex related to clathrin adaptors
    • Dell'Angelica E.C., Mullins C., and Bonifacino J.S. AP-4, a novel protein complex related to clathrin adaptors. J. Biol. Chem. 274 11 (1999) 7278-7285
    • (1999) J. Biol. Chem. , vol.274 , Issue.11 , pp. 7278-7285
    • Dell'Angelica, E.C.1    Mullins, C.2    Bonifacino, J.S.3
  • 12
    • 0031690758 scopus 로고    scopus 로고
    • The herpes simplex virus gE-gI complex facilitates cell-to-cell spread and binds to components of cell junctions
    • Dingwell K.S., and Johnson D.C. The herpes simplex virus gE-gI complex facilitates cell-to-cell spread and binds to components of cell junctions. J. Virol. 72 11 (1998) 8933-8942
    • (1998) J. Virol. , vol.72 , Issue.11 , pp. 8933-8942
    • Dingwell, K.S.1    Johnson, D.C.2
  • 13
    • 0028089018 scopus 로고
    • Herpes simplex virus glycoproteins E and I facilitate cell-to-cell spread in vivo and across junctions of cultured cells
    • Dingwell K.S., Brunetti C.R., Hendricks R.L., Tang Q., Tang M., Rainbow A.J., and Johnson D.C. Herpes simplex virus glycoproteins E and I facilitate cell-to-cell spread in vivo and across junctions of cultured cells. J. Virol. 68 2 (1994) 834-845
    • (1994) J. Virol. , vol.68 , Issue.2 , pp. 834-845
    • Dingwell, K.S.1    Brunetti, C.R.2    Hendricks, R.L.3    Tang, Q.4    Tang, M.5    Rainbow, A.J.6    Johnson, D.C.7
  • 14
    • 33645221124 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at early times and then redistribute to cell junctions to promote cell-cell spread
    • Farnsworth A., and Johnson D.C. Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at early times and then redistribute to cell junctions to promote cell-cell spread. J. Virol. 80 7 (2006) 3167-3179
    • (2006) J. Virol. , vol.80 , Issue.7 , pp. 3167-3179
    • Farnsworth, A.1    Johnson, D.C.2
  • 15
    • 0038447107 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm
    • Farnsworth A., Goldsmith K., and Johnson D.C. Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm. J. Virol. 77 15 (2003) 8481-8494
    • (2003) J. Virol. , vol.77 , Issue.15 , pp. 8481-8494
    • Farnsworth, A.1    Goldsmith, K.2    Johnson, D.C.3
  • 16
    • 33845775712 scopus 로고    scopus 로고
    • Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gD
    • Farnsworth A., Wisner T.W., and Johnson D.C. Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gD. J. Virol. 81 1 (2007) 319-331
    • (2007) J. Virol. , vol.81 , Issue.1 , pp. 319-331
    • Farnsworth, A.1    Wisner, T.W.2    Johnson, D.C.3
  • 17
    • 34250864963 scopus 로고    scopus 로고
    • Epstein-Barr virus B95.8 produced in 293 cells shows marked tropism for differentiated primary epithelial cells and reveals interindividual variation in susceptibility to viral infection
    • Feederle R., Neuhierl B., Bannert H., Geletneky K., Shannon-Lowe C., and Delecluse H.J. Epstein-Barr virus B95.8 produced in 293 cells shows marked tropism for differentiated primary epithelial cells and reveals interindividual variation in susceptibility to viral infection. Int. J. Cancer 121 3 (2007) 588-594
    • (2007) Int. J. Cancer , vol.121 , Issue.3 , pp. 588-594
    • Feederle, R.1    Neuhierl, B.2    Bannert, H.3    Geletneky, K.4    Shannon-Lowe, C.5    Delecluse, H.J.6
  • 18
    • 16844374089 scopus 로고    scopus 로고
    • The building blocks for basolateral vesicles in polarized epithelial cells
    • Folsch H. The building blocks for basolateral vesicles in polarized epithelial cells. Trends Cell Biol. 15 4 (2005) 222-228
    • (2005) Trends Cell Biol. , vol.15 , Issue.4 , pp. 222-228
    • Folsch, H.1
  • 19
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Folsch H., Ohno H., Bonifacino J.S., and Mellman I. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99 2 (1999) 189-198
    • (1999) Cell , vol.99 , Issue.2 , pp. 189-198
    • Folsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 20
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Folsch H., Pypaert M., Schu P., and Mellman I. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J. Cell Biol. 152 3 (2001) 595-606
    • (2001) J. Cell Biol. , vol.152 , Issue.3 , pp. 595-606
    • Folsch, H.1    Pypaert, M.2    Schu, P.3    Mellman, I.4
  • 21
    • 0242266915 scopus 로고    scopus 로고
    • The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains
    • Folsch H., Pypaert M., Maday S., Pelletier L., and Mellman I. The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J. Cell Biol. 163 2 (2003) 351-362
    • (2003) J. Cell Biol. , vol.163 , Issue.2 , pp. 351-362
    • Folsch, H.1    Pypaert, M.2    Maday, S.3    Pelletier, L.4    Mellman, I.5
  • 22
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicella-zoster virus final envelopment in the trans-Golgi network
    • Gershon A.A., Sherman D.L., Zhu Z., Gabel C.A., Ambron R.T., and Gershon M.D. Intracellular transport of newly synthesized varicella-zoster virus final envelopment in the trans-Golgi network. J. Virol. 68 10 (1994) 6372-6390
    • (1994) J. Virol. , vol.68 , Issue.10 , pp. 6372-6390
    • Gershon, A.A.1    Sherman, D.L.2    Zhu, Z.3    Gabel, C.A.4    Ambron, R.T.5    Gershon, M.D.6
  • 23
    • 46349083027 scopus 로고    scopus 로고
    • A gamma-herpesvirus glycoprotein complex manipulates actin to promote viral spread
    • Gill M.B., Edgar R., May J.S., and Stevenson P.G. A gamma-herpesvirus glycoprotein complex manipulates actin to promote viral spread. PLoS ONE 3 3 (2008) e1808
    • (2008) PLoS ONE , vol.3 , Issue.3
    • Gill, M.B.1    Edgar, R.2    May, J.S.3    Stevenson, P.G.4
  • 24
    • 57049144773 scopus 로고    scopus 로고
    • The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope protein whose processing is dependent on coexpression with the BMRF2 protein
    • Gore M., and Hutt-Fletcher L.M. The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope protein whose processing is dependent on coexpression with the BMRF2 protein. Virology 383 1 (2009) 162-167
    • (2009) Virology , vol.383 , Issue.1 , pp. 162-167
    • Gore, M.1    Hutt-Fletcher, L.M.2
  • 25
    • 0031111668 scopus 로고    scopus 로고
    • Oral manifestations of HIV infection
    • Greenspan D., and Greenspan J.S. Oral manifestations of HIV infection. AIDS Clin. Care 9 4 (1997) 29-33
    • (1997) AIDS Clin. Care , vol.9 , Issue.4 , pp. 29-33
    • Greenspan, D.1    Greenspan, J.S.2
  • 26
    • 0022353117 scopus 로고
    • Replication of Epstein-Barr virus within the epithelial cells of oral "hairy" leukoplakia, an AIDS-associated lesion
    • Greenspan J.S., Greenspan D., Lennette E.T., Abrams D.I., Conant M.A., Petersen V., and Freese U.K. Replication of Epstein-Barr virus within the epithelial cells of oral "hairy" leukoplakia, an AIDS-associated lesion. N. Engl. J. Med. 313 25 (1985) 1564-1571
    • (1985) N. Engl. J. Med. , vol.313 , Issue.25 , pp. 1564-1571
    • Greenspan, J.S.1    Greenspan, D.2    Lennette, E.T.3    Abrams, D.I.4    Conant, M.A.5    Petersen, V.6    Freese, U.K.7
  • 27
    • 0023094805 scopus 로고
    • Relation of oral hairy leukoplakia to infection with the human immunodeficiency virus and the risk of developing AIDS
    • Greenspan D., Greenspan J.S., Hearst N.G., Pan L.Z., Conant M.A., Abrams D.I., Hollander H., and Levy J.A. Relation of oral hairy leukoplakia to infection with the human immunodeficiency virus and the risk of developing AIDS. J. Infect. Dis 155 3 (1987) 475-481
    • (1987) J. Infect. Dis , vol.155 , Issue.3 , pp. 475-481
    • Greenspan, D.1    Greenspan, J.S.2    Hearst, N.G.3    Pan, L.Z.4    Conant, M.A.5    Abrams, D.I.6    Hollander, H.7    Levy, J.A.8
  • 28
    • 0028172879 scopus 로고
    • Local increase of beta 1-integrin expression in cocultures of immortalized hepatocytes and sinusoidal endothelial cells
    • Henning W., Bohn W., Nebe B., Knopp A., Rychly J., and Strauss M. Local increase of beta 1-integrin expression in cocultures of immortalized hepatocytes and sinusoidal endothelial cells. Eur. J. Cell Biol. 65 1 (1994) 189-199
    • (1994) Eur. J. Cell Biol. , vol.65 , Issue.1 , pp. 189-199
    • Henning, W.1    Bohn, W.2    Nebe, B.3    Knopp, A.4    Rychly, J.5    Strauss, M.6
  • 29
    • 0025939214 scopus 로고
    • Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinant
    • Hunziker W., Harter C., Matter K., and Mellman I. Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinant. Cell 66 5 (1991) 907-920
    • (1991) Cell , vol.66 , Issue.5 , pp. 907-920
    • Hunziker, W.1    Harter, C.2    Matter, K.3    Mellman, I.4
  • 30
    • 0036133058 scopus 로고    scopus 로고
    • Directed egress of animal viruses promotes cell-to-cell spread
    • Johnson D.C., and Huber M.T. Directed egress of animal viruses promotes cell-to-cell spread. J. Virol. 76 1 (2002) 1-8
    • (2002) J. Virol. , vol.76 , Issue.1 , pp. 1-8
    • Johnson, D.C.1    Huber, M.T.2
  • 31
    • 0035158723 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread
    • Johnson D.C., Webb M., Wisner T.W., and Brunetti C. Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread. J. Virol. 75 2 (2001) 821-833
    • (2001) J. Virol. , vol.75 , Issue.2 , pp. 821-833
    • Johnson, D.C.1    Webb, M.2    Wisner, T.W.3    Brunetti, C.4
  • 32
    • 0000942112 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams and Willkins, New York
    • Kieff E., and Rickinson A. Epstein-Barr virus and its replication. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology." 4th ed. Epstein-Barr virus and its replication (2001), Lippincott Williams and Willkins, New York
    • (2001) Fields Virology." 4th ed. Epstein-Barr virus and its replication
    • Kieff, E.1    Rickinson, A.2
  • 33
    • 0017755779 scopus 로고
    • Replication of EBV in epithelial cells during infectious mononucleosis
    • Lemon S.M., Hutt L.M., Shaw J.E., Li J.L., and Pagano J.S. Replication of EBV in epithelial cells during infectious mononucleosis. Nature 268 5617 (1977) 268-270
    • (1977) Nature , vol.268 , Issue.5617 , pp. 268-270
    • Lemon, S.M.1    Hutt, L.M.2    Shaw, J.E.3    Li, J.L.4    Pagano, J.S.5
  • 34
  • 35
    • 0026061088 scopus 로고
    • Polarized expression of integrin receptors (alpha 6 beta 4, alpha 2 beta 1, alpha 3 beta 1, and alpha v beta 5) and their relationship with the cytoskeleton and basement membrane matrix in cultured human keratinocytes
    • Marchisio P.C., Bondanza S., Cremona O., Cancedda R., and De Luca M. Polarized expression of integrin receptors (alpha 6 beta 4, alpha 2 beta 1, alpha 3 beta 1, and alpha v beta 5) and their relationship with the cytoskeleton and basement membrane matrix in cultured human keratinocytes. J. Cell Biol. 112 4 (1991) 761-773
    • (1991) J. Cell Biol. , vol.112 , Issue.4 , pp. 761-773
    • Marchisio, P.C.1    Bondanza, S.2    Cremona, O.3    Cancedda, R.4    De Luca, M.5
  • 36
    • 23844517401 scopus 로고    scopus 로고
    • Intercellular gamma-herpesvirus dissemination involves co-ordinated intracellular membrane protein transport
    • May J.S., de Lima B.D., Colaco S., and Stevenson P.G. Intercellular gamma-herpesvirus dissemination involves co-ordinated intracellular membrane protein transport. Traffic 6 9 (2005) 780-793
    • (2005) Traffic , vol.6 , Issue.9 , pp. 780-793
    • May, J.S.1    de Lima, B.D.2    Colaco, S.3    Stevenson, P.G.4
  • 37
    • 16244423337 scopus 로고    scopus 로고
    • The murine gammaherpesvirus 68 ORF27 gene product contributes to intercellular viral spread
    • May J.S., Walker J., Colaco S., and Stevenson P.G. The murine gammaherpesvirus 68 ORF27 gene product contributes to intercellular viral spread. J. Virol. 79 8 (2005) 5059-5068
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 5059-5068
    • May, J.S.1    Walker, J.2    Colaco, S.3    Stevenson, P.G.4
  • 38
    • 0035138826 scopus 로고    scopus 로고
    • Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions
    • McMillan T.N., and Johnson D.C. Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions. J. Virol. 75 4 (2001) 1928-1940
    • (2001) J. Virol. , vol.75 , Issue.4 , pp. 1928-1940
    • McMillan, T.N.1    Johnson, D.C.2
  • 39
    • 0026316328 scopus 로고
    • Epstein-Barr virus infection in oral hairy leukoplakia: virus replication in the absence of a detectable latent phase
    • Niedobitek G., Young L.S., Lau R., Brooks L., Greenspan D., Greenspan J.S., and Rickinson A.B. Epstein-Barr virus infection in oral hairy leukoplakia: virus replication in the absence of a detectable latent phase. J. Gen. Virol. 72 Pt 12 (1991) 3035-3046
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 12 , pp. 3035-3046
    • Niedobitek, G.1    Young, L.S.2    Lau, R.3    Brooks, L.4    Greenspan, D.5    Greenspan, J.S.6    Rickinson, A.B.7
  • 42
    • 7644222272 scopus 로고    scopus 로고
    • Epstein-Barr virus infection in ex vivo tonsil epithelial cell cultures of asymptomatic carriers
    • Pegtel D.M., Middeldorp J., and Thorley-Lawson D.A. Epstein-Barr virus infection in ex vivo tonsil epithelial cell cultures of asymptomatic carriers. J. Virol. 78 22 (2004) 12613-12624
    • (2004) J. Virol. , vol.78 , Issue.22 , pp. 12613-12624
    • Pegtel, D.M.1    Middeldorp, J.2    Thorley-Lawson, D.A.3
  • 43
    • 0023280687 scopus 로고
    • Polarized distribution of integrin and fibronectin in retinal pigment epithelium
    • Philp N.J., and Nachmias V.T. Polarized distribution of integrin and fibronectin in retinal pigment epithelium. Investig. Ophthalmol. Vis. Sci. 28 8 (1987) 1275-1280
    • (1987) Investig. Ophthalmol. Vis. Sci. , vol.28 , Issue.8 , pp. 1275-1280
    • Philp, N.J.1    Nachmias, V.T.2
  • 44
    • 24644490502 scopus 로고    scopus 로고
    • The extracellular domain of herpes simplex virus gE is indispensable for efficient cell-to-cell spread: evidence for gE/gI receptors
    • Polcicova K., Goldsmith K., Rainish B.L., Wisner T.W., and Johnson D.C. The extracellular domain of herpes simplex virus gE is indispensable for efficient cell-to-cell spread: evidence for gE/gI receptors. J. Virol. 79 18 (2005) 11990-12001
    • (2005) J. Virol. , vol.79 , Issue.18 , pp. 11990-12001
    • Polcicova, K.1    Goldsmith, K.2    Rainish, B.L.3    Wisner, T.W.4    Johnson, D.C.5
  • 46
    • 0034737482 scopus 로고    scopus 로고
    • Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface
    • Renold A., Cescato R., Beuret N., Vogel L.K., Wahlberg J.M., Brown J.L., Fiedler K., and Spiess M. Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface. J. Biol. Chem. 275 13 (2000) 9290-9295
    • (2000) J. Biol. Chem. , vol.275 , Issue.13 , pp. 9290-9295
    • Renold, A.1    Cescato, R.2    Beuret, N.3    Vogel, L.K.4    Wahlberg, J.M.5    Brown, J.L.6    Fiedler, K.7    Spiess, M.8
  • 47
    • 0021258132 scopus 로고
    • Epstein-Barr virus in epithelium
    • Rickinson A. Epstein-Barr virus in epithelium. Nature 310 5973 (1984) 99-100
    • (1984) Nature , vol.310 , Issue.5973 , pp. 99-100
    • Rickinson, A.1
  • 48
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr Virus
    • Fields B.N., Knipe D.M., and Howley P.M. (Eds), Lippincott-Williams and Wilkins, Philadelphia
    • Rickinson A., and Kieff E. Epstein-Barr Virus. In: Fields B.N., Knipe D.M., and Howley P.M. (Eds). Fields Virology." Epstein-Barr Virus Vol. 2 (2001), Lippincott-Williams and Wilkins, Philadelphia
    • (2001) Fields Virology." Epstein-Barr Virus , vol.2
    • Rickinson, A.1    Kieff, E.2
  • 49
    • 54149119141 scopus 로고    scopus 로고
    • Avoiding the void: cell-to-cell spread of human viruses
    • Sattentau Q. Avoiding the void: cell-to-cell spread of human viruses. Nat. Rev., Microbiol. 6 11 (2008) 815-826
    • (2008) Nat. Rev., Microbiol. , vol.6 , Issue.11 , pp. 815-826
    • Sattentau, Q.1
  • 50
    • 0033959784 scopus 로고    scopus 로고
    • Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs
    • Sevier C.S., Weisz O.A., Davis M., and Machamer C.E. Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs. Mol. Biol. Cell 11 1 (2000) 13-22
    • (2000) Mol. Biol. Cell , vol.11 , Issue.1 , pp. 13-22
    • Sevier, C.S.1    Weisz, O.A.2    Davis, M.3    Machamer, C.E.4
  • 51
    • 0036167130 scopus 로고    scopus 로고
    • AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells
    • Simmen T., Honing S., Icking A., Tikkanen R., and Hunziker W. AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. Nat. Cell Biol. 21 21 (2002)
    • (2002) Nat. Cell Biol. , vol.21 , Issue.21
    • Simmen, T.1    Honing, S.2    Icking, A.3    Tikkanen, R.4    Hunziker, W.5
  • 52
  • 54
    • 0035024157 scopus 로고    scopus 로고
    • Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment → deenvelopment → reenvelopment pathway
    • Skepper J.N., Whiteley A., Browne H., and Minson A. Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment → deenvelopment → reenvelopment pathway. J. Virol. 75 12 (2001) 5697-5702
    • (2001) J. Virol. , vol.75 , Issue.12 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 55
    • 0031901313 scopus 로고    scopus 로고
    • Role of envelope protein gE endocytosis in the pseudorabies virus life cycle
    • Tirabassi R.S., and Enquist L.W. Role of envelope protein gE endocytosis in the pseudorabies virus life cycle. J. Virol. 72 6 (1998) 4571-4579
    • (1998) J. Virol. , vol.72 , Issue.6 , pp. 4571-4579
    • Tirabassi, R.S.1    Enquist, L.W.2
  • 56
    • 0032976556 scopus 로고    scopus 로고
    • Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE
    • Tirabassi R.S., and Enquist L.W. Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE. J. Virol. 73 4 (1999) 2717-2728
    • (1999) J. Virol. , vol.73 , Issue.4 , pp. 2717-2728
    • Tirabassi, R.S.1    Enquist, L.W.2
  • 57
    • 0030051976 scopus 로고    scopus 로고
    • Role of apical and basolateral membranes in replication of human cytomegalovirus in polarized retinal pigment epithelial cells
    • Tugizov S., Maidji E., and Pereira L. Role of apical and basolateral membranes in replication of human cytomegalovirus in polarized retinal pigment epithelial cells. J. Gen. Virol. 77 Pt 1 (1996) 61-74
    • (1996) J. Gen. Virol. , vol.77 , Issue.PART 1 , pp. 61-74
    • Tugizov, S.1    Maidji, E.2    Pereira, L.3
  • 58
    • 0031846860 scopus 로고    scopus 로고
    • Human cytomegalovirus glycoprotein B contains autonomous determinants for vectorial targeting to apical membranes of polarized epithelial cells
    • Tugizov S., Maidji E., Xiao J., Zheng Z., and Pereira L. Human cytomegalovirus glycoprotein B contains autonomous determinants for vectorial targeting to apical membranes of polarized epithelial cells. J. Virol. 72 (1998) 7374-7386
    • (1998) J. Virol. , vol.72 , pp. 7374-7386
    • Tugizov, S.1    Maidji, E.2    Xiao, J.3    Zheng, Z.4    Pereira, L.5
  • 59
    • 0037349930 scopus 로고    scopus 로고
    • Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells
    • Tugizov S.M., Berline J.W., and Palefsky J.M. Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells. Nat. Med. 9 3 (2003) 307-314
    • (2003) Nat. Med. , vol.9 , Issue.3 , pp. 307-314
    • Tugizov, S.M.1    Berline, J.W.2    Palefsky, J.M.3
  • 60
    • 34249801515 scopus 로고    scopus 로고
    • Epstein-Barr virus (EBV)-infected monocytes facilitate dissemination of EBV within the oral mucosal epithelium
    • Tugizov S., Herrera R., Veluppillai P., Greenspan J., Greenspan D., and Palefsky J.M. Epstein-Barr virus (EBV)-infected monocytes facilitate dissemination of EBV within the oral mucosal epithelium. J. Virol. 81 11 (2007) 5484-5496
    • (2007) J. Virol. , vol.81 , Issue.11 , pp. 5484-5496
    • Tugizov, S.1    Herrera, R.2    Veluppillai, P.3    Greenspan, J.4    Greenspan, D.5    Palefsky, J.M.6
  • 61
    • 21644443202 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress
    • Turcotte S., Letellier J., and Lippe R. Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress. J. Virol. 79 14 (2005) 8847-8860
    • (2005) J. Virol. , vol.79 , Issue.14 , pp. 8847-8860
    • Turcotte, S.1    Letellier, J.2    Lippe, R.3
  • 62
    • 0032829388 scopus 로고    scopus 로고
    • Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network
    • Whiteley A., Bruun B., Minson T., and Browne H. Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network. J. Virol. 73 11 (1999) 9515-9520
    • (1999) J. Virol. , vol.73 , Issue.11 , pp. 9515-9520
    • Whiteley, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 63
    • 33847058145 scopus 로고    scopus 로고
    • Characterization of the Epstein-Barr virus glycoprotein BMRF-2
    • Xiao J., Palefsky J.M., Herrera R., and Tugizov S.M. Characterization of the Epstein-Barr virus glycoprotein BMRF-2. Virology 359 2 (2007) 382-396
    • (2007) Virology , vol.359 , Issue.2 , pp. 382-396
    • Xiao, J.1    Palefsky, J.M.2    Herrera, R.3    Tugizov, S.M.4
  • 64
    • 36549087307 scopus 로고    scopus 로고
    • The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral epithelial cells
    • Xiao J., Palefsky J.M., Herrera R., Berline J., and Tugizov S.M. The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral epithelial cells. Virology 370 2 (2008) 430-442
    • (2008) Virology , vol.370 , Issue.2 , pp. 430-442
    • Xiao, J.1    Palefsky, J.M.2    Herrera, R.3    Berline, J.4    Tugizov, S.M.5
  • 66
    • 0029794452 scopus 로고    scopus 로고
    • Targeting of glycoprotein I (gE) of varicella-zoster virus to the trans-Golgi network by an AYRV sequence and an acidic amino acid-rich patch in the cytosolic domain of the molecule
    • Zhu Z., Hao Y., Gershon M.D., Ambron R.T., and Gershon A.A. Targeting of glycoprotein I (gE) of varicella-zoster virus to the trans-Golgi network by an AYRV sequence and an acidic amino acid-rich patch in the cytosolic domain of the molecule. J. Virol. 70 10 (1996) 6563-6575
    • (1996) J. Virol. , vol.70 , Issue.10 , pp. 6563-6575
    • Zhu, Z.1    Hao, Y.2    Gershon, M.D.3    Ambron, R.T.4    Gershon, A.A.5


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