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7 - Entry of alphaherpesviruses into the cell

from Part II - Basic virology and viral gene effects on host cell functions: alphaherpesviruses

Published online by Cambridge University Press:  24 December 2009

By
Gabriella Campadelli-Fiume  and
Laura Menotti
Edited by
Ann Arvin ,
Gabriella Campadelli-Fiume ,
Edward Mocarski ,
Patrick S. Moore ,
Bernard Roizman ,
Richard Whitley  and
Koichi Yamanishi
Gabriella Campadelli-Fiume
Affiliation:
Department of Experimental Pathology, Alma Mater Studiorum-University of Bologna, Italy
Laura Menotti
Affiliation:
Department of Experimental Pathology, Alma Mater Studiorum-University of Bologna, Italy
Ann Arvin
Affiliation:
Stanford University, California
Gabriella Campadelli-Fiume
Affiliation:
Università degli Studi, Bologna, Italy
Edward Mocarski
Affiliation:
Emory University, Atlanta
Patrick S. Moore
Affiliation:
University of Pittsburgh
Bernard Roizman
Affiliation:
University of Chicago
Richard Whitley
Affiliation:
University of Alabama, Birmingham
Koichi Yamanishi
Affiliation:
University of Osaka, Japan
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Summary

Introduction

Herpes simplex virus (HSV) represents the most comprehensive example of virus-receptor interaction in the Herpesviridae family, and the prototype virus encoding multipartite entry genes. Whereas small enveloped viruses package the functions required for entry and fusion into one or two fusion glycoproteins, in HSV the same functions are distributed over several distinct glycoproteins, each with a specialized activity. In addition, HSV encodes a highly sophisticated system for promoting and blocking fusion between the viral envelope and cell membrane. Because the most obvious models of virus entry into the cell do not fit with the HSV complexity, and despite our detailed knowledge of the HSV receptors and of the crystal structure of glycoprotein D (gD), the receptor-binding glycoprotein, and of gB, HSV entry is still, in part, a puzzle (WuDunn and Spear, 1989; Cocchi et al., 1998b; Geraghty et al., 1998; Carfi et al., 2001).

The current model of HSV entry envisions that, first, the virus attaches to cell membranes by the interaction of gC, and possibly gB, to glycosaminoglycans (GAGs) (Herold et al., 1991). This binding likely creates multiple points of adhesion, is reversible, and the detached virus maintains its infectivity, indicating that fusion has yet to take place. Penetration requires gD, whose ectodomain contains two physically separate and functionally distinct regions, i.e., the region made of the N-terminus that carries the receptor-binding sites, and the C-terminus that carries the profusion domain (Ligas and Johnson, 1988; Cocchi et al., 2004).

Type
Chapter
Information
Human Herpesviruses
Biology, Therapy, and Immunoprophylaxis
 , pp. 93 - 111
Publisher: Cambridge University Press
Print publication year: 2007

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References

Avitabile, E., Ward, P. L., Lazzaro, C., Torrisi, M. R., Roizman, B., and Campadelli-Fiume, G. (1994). The herpes simplex virus UL20 protein compensates for the differential disruption of exocytosis of virions and membrane glycoproteins associated with fragmentation of the Golgi apparatus. J. Virol., 68, 7397–7405.Google ScholarPubMed
Avitabile, E., Lombardi, G., and Campadelli-Fiume, G. (2003). Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell–cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH and gL. J. Virol., 77, 6836–6844.CrossRefGoogle Scholar
Avitabile, E., Lombardi, G., Gianni, T., Capri, M., and Campadelli-Fiume, G. (2004). Coexpression of UL20p and gK inhibits cell–cell fusion mediated by herpes simplex virus glycoproteins gD, gH-gL, and wt-gB or an endocytosis-defective gB mutant, and downmodulates their cell surface expression. J. Virol., 78, 8015–8025.CrossRefGoogle ScholarPubMed
Baines, J. D., Ward, P. L., Campadelli-Fiume, G., and Roizman, B. (1991). The UL20 gene of herpes simplex virus 1 encodes a function necessary for viral egress. J. Virol., 65, 6414–6424.Google ScholarPubMed
Batterson, W., Furlong, D., and Roizman, B. (1983). Molecular genetics of herpes simplex virus. VIII. Further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle. J. Virol., 45, 397–407.Google ScholarPubMed
Beitia Ortiz de Zarate, I., Kaelin, K., and Rozenberg, F. (2004). Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity. J. Virol., 78, 1540–1551.CrossRefGoogle ScholarPubMed
Bender, F. C., Whitbeck, J. C., Ponce de Leon, M., Lou, H., Eisenberg, R. J., and Cohen, G. H. (2003). Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry. J. Virol., 77, 9542–9552.CrossRefGoogle ScholarPubMed
Browne, H., Bruun, B., Whiteley, A., and Minson, T. (2003). Analysis of the role of the membrane-spanning and cytoplasmic tail domains of herpes simplex virus type 1 glycoprotein D in membrane fusion. J. Gen. Virol., 84, 1085–1089.CrossRefGoogle ScholarPubMed
Bzik, D. J., Fox, B. A., DeLuca, N. A., and Person, S. (1984). Nucleotide sequence of a region of the herpes simplex virus type 1 gB glycoprotein gene: mutations affecting rate of virus entry and cell fusion. Virology, 137, 185–190.CrossRefGoogle ScholarPubMed
Cai, W. Z., Person, S., Warner, S. C., Zhou, J. H., and DeLuca, N. A. (1987). Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1. J. Virol., 61, 714–721.Google Scholar
Cai, W. Z., Gu, B., and Person, S. (1988). Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion [published erratum appears in J. Virol. 1988 Nov; 62(11):4438]. J. Virol., 62, 2596–2604.Google Scholar
Campadelli-Fiume, G., Arsenakis, M., Farabegoli, F., and Roizman, B. (1988). Entry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virus. J. Virol., 62, 159–167.Google Scholar
Campadelli-Fiume, G., Stirpe, D., Boscaro, A.et al. (1990). Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection. Virology, 178, 213–222.CrossRefGoogle Scholar
Campadelli-Fiume, G., Cocchi, F., Menotti, L., and Lopez, M. (2000). The novel receptors that mediate the entry of herpes simplex viruses and animal alphaherpesviruses into cells. Rev. Med. Virol., 10, 305–319.3.0.CO;2-T>CrossRefGoogle Scholar
Carfi, A., Willis, S. H., Whitbeck, J. C.et al. (2001). Herpes simplex virus glycoprotein D bound to the human receptor HveA. Mol. Cell, 8, 169–179.CrossRefGoogle ScholarPubMed
Cocchi, F., Lopez, M., Menotti, L., Aoubala, M., Dubreuil, P., and Campadelli-Fiume, G. (1998a). The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D. Proc. Natl Acad. Sci. USA, 95, 15700–15705.CrossRefGoogle Scholar
Cocchi, F., Menotti, L., Mirandola, P., Lopez, M., and Campadelli-Fiume, G. (1998b). The ectodomain of a novel member of the immunoglobulin superfamily related to the poliovirus receptor has the attibutes of a bonafide receptor for herpes simplex viruses 1 and 2 in human cells. J. Virol., 72, 9992–10002.Google Scholar
Cocchi, F., Lopez, M., Dubreuil, P., Campadelli-Fiume, G., and Menotti, L. (2001). Chimeric nectin1-poliovirus receptor molecules identify a nectin1 region functional in herpes simplex virus entry. J. Virol., 75, 7987–7994.CrossRefGoogle ScholarPubMed
Cocchi, F., Fusco, D., Menotti, L.et al. (2004). The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry. Proc. Natl Acad. Sci. USA, 101, 7445–7450.CrossRefGoogle ScholarPubMed
Connolly, S. A., Whitbeck, J. J., Rux, A. H.et al. (2001). Glycoprotein D homologs in herpes simplex virus type 1, pseudorabies virus, and bovine herpes virus type 1 bind directly to human HveC(nectin-1) with different affinities. Virology, 280, 7–18.CrossRefGoogle ScholarPubMed
Connolly, S. A., Landsburg, D. J., Carfi, A., Wiley, D. C., Eisenberg, R. J., and Cohen, G. H. (2002). Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM). J. Virol., 76, 10894–10904.CrossRefGoogle Scholar
Connolly, S. A., Landsburg, D. J., Carfi, A., Wiley, D. C., Cohen, G. H., and Eisenberg, R. J. (2003). Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/ HVEM binding interface. J. Virol., 77, 8127–8140.CrossRefGoogle ScholarPubMed
Connolly, S. A., Landsburg, D. J., Carfi, A.et al. (2005). Potential nectin-1 binding site on herpes simplex virus glycoprotein D. J. Virol., 79, 1282–1295.CrossRefGoogle ScholarPubMed
Davison, A. J. and Scott, J. E. (1986). The complete DNA sequence of varicella-zoster virus. J. Gen. Virol., 67(9), 1759–1816.CrossRefGoogle ScholarPubMed
Desai, P. J., Schaffer, P. A., and Minson, A. C. (1988). Excretion of non-infectious virus particles lacking glycoprotein H by a temperature-sensitive mutant of herpes simplex virus type 1: evidence that gH is essential for virion infectivity. J. Gen. Virol., 69(6), 1147–1156.CrossRefGoogle Scholar
Diefenbach, R. J., Miranda-Saksena, M., Diefenbach, E.et al. (2002). Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain. J. Virol., 76, 3282–3291.CrossRefGoogle ScholarPubMed
Döhner, K. and Sodeik, B. (2005). The role of the cytoskeleton during viral infection. Curr. Top. Microbiol. Immunol., 285, 67–108.Google Scholar
Döhner, K., Wolfstein, A., Prank, U.et al. (2002). Function of dynein and dynactin in herpes simplex virus capsid transport. Mol. Biol. Cell, 13, 2795–2809.Google Scholar
Dolter, K. E., Goins, W. F., Levine, M., and Glorioso, J. C. (1992). Genetic analysis of type-specific antigenic determinants of herpes simplex virus glycoprotein C. J. Virol., 66, 4864–4873.Google ScholarPubMed
Duus, K. M. and Grose, C. (1996). Multiple regulatory effects of varicella-zoster virus (VZV) gL on trafficking patterns and fusogenic properties of VZV gH. J. Virol., 70, 8961–8971.Google ScholarPubMed
Duus, K. M., Hatfield, C., and Grose, C. (1995). Cell surface expression and fusion by the varicella-zoster virus gH:gL glycoprotein complex: analysis by laser scanning confocal microscopy. Virology, 210, 429–440.CrossRefGoogle ScholarPubMed
Enquist, L. W., Husak, P. J., Banfield, B. W., and Smith, G. A. (1998). Infection and spread of alphaherpesviruses in the nervous system. Adv. Virus Res., 51, 237–247.CrossRefGoogle Scholar
Fan, Z., Grantham, M. L., Smith, M. S., Anderson, E. S., Cardelli, J. A., and Muggeridge, M. I. (2002). Truncation of herpes simplex virus type 2 glycoprotein B increases its cell surface expression and activity in cell–cell fusion, but these properties are unrelated. J. Virol., 76, 9271–9283.CrossRefGoogle ScholarPubMed
Foà-Tomasi, L., Avitabile, E., Boscaro, A.et al. (1991). Herpes simplex virus (HSV) glycoprotein H is partially processed in a cell line that expresses the glycoprotein and fully processed in cells infected with deletion or ts mutants in the known HSV glycoproteins. Virology, 180, 474–482.CrossRefGoogle Scholar
Forghani, B., Ni, L., and Grose, C. (1994). Neutralization epitope of the varicella-zoster virus gH:gL glycoprotein complex. Virology, 199, 458–462.CrossRefGoogle ScholarPubMed
Forrester, A., Farrell, H., Wilkinson, G., Kaye, J., Poynter, Davis N., and Minson, T. (1992). Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted. J. Virol., 66, 341–348.Google ScholarPubMed
Foster, T. P. and Kousoulas, K. G. (1999). Genetic analysis of the role of herpes simplex virus type 1 glycoprotein K in infectious virus production and egress. J. Virol., 73, 8457–8468.Google ScholarPubMed
Foster, T. P., Melancon, J., and Kousoulas, K. (2001a). An alpha-helical domain within the carboxyl terminus of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) is associated with cell fusion and resistance to heparin inhibition of cell fusion. Virology, 287, 18–29.CrossRefGoogle Scholar
Foster, T. P., Rybachuk, G. V., and Kousoulas, K. G. (2001b). Glycoprotein K specified by herpes simplex virus type 1 is expressed on virions as a Golgi complex-dependent glycosylated species and functions in virion entry. J. Virol., 75, 12431–12438.CrossRefGoogle Scholar
Foster, T. P., Alvarez, X., and Kousoulas, K. G. (2003a). Plasma membrane topology of syncytial domains of herpes simplex virus type 1 glycoprotein K (gK): the UL20 protein enables cell surface localization of gK but not gK-mediated cell-to-cell fusion. J. Virol., 77, 499–510.CrossRefGoogle Scholar
Foster, T. P., Rybachuk, G. V., Alvarez, X., Borkhsenious, O., and Kousoulas, K. G. (2003b). Overexpression of gK in gK-transformed cells collapses the Golgi apparatus into the endoplasmic reticulum inhibiting virion egress, glycoprotein transport, and virus-induced cell fusion. Virology, 317, 237–252.CrossRefGoogle Scholar
Foster, T. P., Melancon, J. M., Baines, J. D., and Kousoulas, K. G. (2004). The herpes simplex virus type 1 UL20 protein modulates membrane fusion events during cytoplasmic virion morphogenesis and virus-induced cell fusion. J. Virol., 78, 5347–5357.CrossRefGoogle ScholarPubMed
Fuller, A. O., Santos, R. E., and Spear, P. G. (1989). Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration. J. Virol., 63, 3435–3443.Google ScholarPubMed
Fusco, D., Forghieri, C., and Campadelli-Fiume, G. (2005). The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors. Proc. Natl Acad. Sci. USA, 102, 9323–9328.CrossRefGoogle Scholar
Galdiero, M., Whiteley, A., Bruun, B., Bell, S., Minson, T., and Browne, H. (1997). Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H. J. Virol., 71, 2163–2170.Google ScholarPubMed
Galdiero, S., Vitiello, M., D'Isanto, M.et al. (2006). Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. J. Gen. Virol., 87, 1085–1097.CrossRefGoogle ScholarPubMed
Geraghty, R. J., Krummenacher, C., Cohen, G. H., Eisenberg, R. J., and Spear, P. G. (1998). Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science, 280, 1618–1620.CrossRefGoogle ScholarPubMed
Gerber, S. I., Belval, B. J., and Herold, B. C. (1995). Differences in the role of glycoprotein C of HSV-1 and HSV-2 in viral binding may contribute to serotype differences in cell tropism. Virology, 214, 29–39.CrossRefGoogle ScholarPubMed
Gianni, T., Campadelli-Fiume, G., and Menotti, L. (2004). Entry of herpes simplex virus mediated by chimeric forms of nectin1 retargeted to endosomes or to lipid rafts occurs through acidic endosomes. J. Virol., 78, 12268–12276.CrossRefGoogle ScholarPubMed
Gianni, T., Martelli, P. L., Casadio, R., and Campadelli-Fiume, G. (2005a). The ectodomain of herpes simpex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the Herpesviridae family. J. Virol., 79, 2931–2940.CrossRefGoogle Scholar
Gianni, T., Menotti, L., and Campadelli-Fiume, G. (2005b). A heptad repeat in herpes simplex virus gH, located downstream of the alpha-helix with attributes of a fusion peptide, is critical for virus entry and fusion. J. Virol., 79, 7042–7049.CrossRefGoogle Scholar
Gianni, T., Fato, R., Bergamini, C., Lenaz, G., and Campadelli-Fiume, G. (2006a). Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion. J. Virol., 80, 8190–8198.CrossRefGoogle Scholar
Gianni, T., Piccoli, A., Bertucci, C., and Campadelli-Fiume, G. (2006b). Heptad repeat 2 in herpes simplex virus-1 gH interacts with heptad repeat 1 and is critical for virus entry and fusion. J. Virol., 80, 2216–2224.CrossRefGoogle Scholar
Gompels, U. and Minson, A. (1986). The properties and sequence of glycoprotein H of herpes simplex virus type 1. Virology, 153, 230–247.CrossRefGoogle ScholarPubMed
Griffiths, A., Renfrey, S., and Minson, T. (1998). Glycoprotein C-deficient mutants of two strains of herpes simplex virus type 1 exhibit unaltered adsorption characteristics on polarized or non-polarized cells. J. Gen. Virol., 79(4), 807–812.CrossRefGoogle ScholarPubMed
Gruenheid, S., Gatzke, L., Meadows, H., and Tufaro, F. (1993). Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans. J. Virol., 67, 93–100.Google Scholar
Grunewald, K., Desai, P., Winkler, D. C.et al. (2003). Three-dimensional structure of herpes simplex virus from cryo-electron tomography. Science, 302, 1396–1398.CrossRefGoogle ScholarPubMed
Haarr, L., Shukla, D., Rodahl, E., Canto, M. C., and Spear, P. G. (2001). Transcription from the gene encoding the herpesvirus entry receptor nectin-1 (HveC) in nervous tissue of adult mouse. Virology, 287, 301–309.CrossRefGoogle ScholarPubMed
Harman, A., Browne, H., and Minson, T. (2002). The transmembrane domain and cytoplasmic tail of herpes simplex virus type 1 glycoprotein H play a role in membrane fusion. J. Virol., 76, 10708–10716.CrossRefGoogle ScholarPubMed
Harrop, J. A., Reddy, M., Dede, K.et al. (1998). Antibodies to TR2 (herpesvirus entry mediator), a new member of the TNF receptor superfamily, block T cell proliferation, expression of activation markers, and production of cytokines. J. Immunol., 161, 1786–1794.Google Scholar
Heineman, T. C. and Hall, S. L. (2001). VZV gB endocytosis and Golgi localization are mediated by YXXphi motifs in its cytoplasmic domain. Virology, 285, 42–49.CrossRefGoogle ScholarPubMed
Heldwein, E. E., Lou, H., Bender, F. C., Cohen, G. H., Eisenberg, R. J., and Harrison, S. C. (2006). Crystal structure of glycoprotein B from herpes simplex virus 1. Science, 313, 217–220.CrossRefGoogle ScholarPubMed
Herold, B. C., WuDunn, D., Soltys, N., and Spear, P. G. (1991). Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol., 65, 1090–1098.Google Scholar
Highlander, S. L., Dorney, D. J., Gage, P. J.et al. (1989). Identification of mar mutations in herpes simplex virus type 1 glycoprotein B which alter antigenic structure and function in virus penetration. J. Virol., 63, 730–738.Google ScholarPubMed
Hutchinson, L. and Johnson, D. C. (1995). Herpes simplex virus glycoprotein K promotes egress of virus particles. J. Virol., 69, 5401–5413.Google ScholarPubMed
Hutchinson, L., Browne, H., Wargent, V.et al. (1992a). A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH. J. Virol., 66, 2240–2250.Google Scholar
Hutchinson, L., Goldsmith, K., Snoddy, D., Ghosh, H., Graham, F. L., and Johnson, D. C. (1992b). Identification and characterization of a novel herpes simplex virus glycoprotein, gK, involved in cell fusion. J. Virol., 66, 5603–5609.Google Scholar
Jogger, C. R., Montgomery, R. I., and Spear, P. G. (2004). Effects of linker-insertion mutations in herpes simplex virus 1 gD on glycoprotein-induced fusion with cells expressing HVEM or nectin-1. Virology, 318, 318–326.CrossRefGoogle ScholarPubMed
Johnson, D. C., Burke, R. L., and Gregory, T. (1990). Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells. J. Virol., 64, 2569–2576.Google ScholarPubMed
Johnson, R. M. and Spear, P. G. (1989). Herpes simplex virus glycoprotein D mediates interference with herpes simplex virus infection. J. Virol., 63, 819–827.Google ScholarPubMed
Jones, N. A. and Geraghty, R. J. (2004). Fusion activity of lipid-anchored envelope glycoproteins of herpes simplex virus type 1. Virology, 324, 213–228.CrossRefGoogle ScholarPubMed
Kaye, J. F., Gompels, U. A., and Minson, A. C. (1992). Glycoprotein H of human cytomegalovirus (HCMV) forms a stable complex with the HCMV UL115 gene product. J. Gen. Virol., 73(10), 2693–2698.CrossRefGoogle ScholarPubMed
Keller, P. M., Neff, B. J., and Ellis, R. W. (1984). Three major glycoprotein genes of varicella-zoster virus whose products have neutralization epitopes. J. Virol., 52, 293–297.Google ScholarPubMed
Kenyon, T. K., Cohen, J. I., and Grose, C. (2002). Phosphorylation by the varicella-zoster virus ORF47 protein serine kinase determines whether endocytosed viral gE traffics to the trans-Golgi network or recycles to the cell membrane. J. Virol., 76, 10980–10993.CrossRefGoogle ScholarPubMed
Kousoulas, K. G., Huo, B., and Pereira, L. (1988). Antibody-resistant mutations in cross-reactive and type-specific epitopes of herpes simplex virus 1 glycoprotein B map in separate domains. Virology, 166, 423–431.CrossRefGoogle ScholarPubMed
Krummenacher, C., Nicola, A. V., Whitbeck, J. C.et al. (1998). Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry. J. Virol., 72, 7064–7074.Google ScholarPubMed
Krummenacher, C., Rux, A. H., Whitbeck, J. C.et al. (1999). The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC. J. Virol., 73, 8127–8137.Google ScholarPubMed
Krummenacher, C., Baribaud, I., Ponce De Leon, M.et al. (2000). Localization of a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies. J. Virol., 74, 10863–10872.CrossRefGoogle ScholarPubMed
Krummenacher, C., Baribaud, I., Ponce De Leon, M.et al. (2004). Comparative usage of herpesvirus entry mediator A and nectin-1 by laboratory strains and clinical isolates of herpes simplex virus. Virology, 322, 286–299.CrossRefGoogle ScholarPubMed
Krummenacher, C., Supekar, V. M., Whitbeck, J. C.et al. (2005). Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. EMBO J., 24, 4144–4153.CrossRefGoogle ScholarPubMed
Kwon, B. S., Tan, K. B., Ni, J.et al. (1997). A newly identified member of the tumor necrosis factor receptor superfamily with a wide tissue distribution and involvement in lymphocyte activation. J. Biol. Chem., 272, 14272–14276.CrossRefGoogle ScholarPubMed
La, S., Kim, J., Kwon, B. S., and Kwon, B. (2002). Herpes simplex virus type 1 glycoprotein D inhibits T-cell proliferation. Mol. Cells, 14, 398–403.Google ScholarPubMed
Ligas, M. W. and Johnson, D. C. (1988). A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells. J. Virol., 62, 1486–1494.Google ScholarPubMed
Linehan, M. M., Richman, S., Krummenacher, C., Eisenberg, R. J., Cohen, G. H., and Iwasaki, A. (2004). In vivo role of nectin-1 in entry of herpes simplex virus type 1 (HSV-1) and HSV-2 through the vaginal mucosa. J. Virol., 78, 2530–2536.CrossRefGoogle ScholarPubMed
Liu, D. X., Gompels, U. A., Foà-Tomasi, L., and Campadelli-Fiume, G. (1993). Human herpesvirus-6 glycoprotein H and L homologs are components of the gp100 complex and the gH external domain is the target for neutralizing monoclonal antibodies. Virology, 197, 12–22.CrossRefGoogle ScholarPubMed
Lopez, M., Cocchi, F., Menotti, L., Avitabile, E., Dubreuil, P., and Campadelli-Fiume, G. (2000). Nectin2a (PRR2a or HveB) and nectin2d are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D. J. Virol., 74, 1267–1274.CrossRefGoogle Scholar
Lopez, M., Cocchi, F., Avitabile, E.et al. (2001). Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or PRR1-HIgR-HveC) modulates positively and negatively susceptibility to HSV infection. J. Virol., 75, 5684–5691.CrossRefGoogle ScholarPubMed
Mabit, H., Nakano, M. Y., Prank, U.et al. (2002). Intact microtubules support adenovirus and herpes simplex virus infections. J. Virol., 76, 9962–9971.CrossRefGoogle ScholarPubMed
Mallory, S., Sommer, M., and Arvin, A. M. (1997). Mutational analysis of the role of glycoprotein I in varicella-zoster virus replication and its effects on glycoprotein E conformation and trafficking. J. Virol., 71, 8279–8288.Google Scholar
Manoj, S., Jogger, C. R., Myscofski, D., Yoon, M., and Spear, P. G. (2004). Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism. Proc. Natl Acad. Sci. USA, 101, 12414–12421.CrossRefGoogle ScholarPubMed
Manservigi, R., Spear, P. G., and Buchan, A. (1977). Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. Proc. Natl Acad. Sci. USA, 74, 3913–3917.CrossRefGoogle ScholarPubMed
Maresova, L., Pasieka, T. J., and Grose, C. (2001). Varicella-zoster Virus gB and gE coexpression, but not gB or gE alone, leads to abundant fusion and syncytium formation equivalent to those from gH and gL coexpression. J. Virol., 75, 9483–9492.CrossRefGoogle ScholarPubMed
Marozin, S., Prank, U., and Sodeik, B. (2004). Herpes simplex virus type 1 infection of polarized epithelial cells requires microtubules and access to receptors at cell–cell contact sites. J. Gen. Virol., 85, 775–786.CrossRefGoogle ScholarPubMed
Martinez, W. M. and Spear, P. G. (2002). Amino acid substitutions in the V domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for Pseudorabies virus or bovine herpesvirus 1. J. Virol., 76, 7255–7262.CrossRefGoogle ScholarPubMed
Mata, M., Zhang, M., Hu, X., and Fink, D. J. (2001). HveC (nectin-1) is expressed at high levels in sensory neurons, but not in motor neurons, of the rat peripheral nervous system. J. Neurovirol., 7, 476–480.Google Scholar
Matsushima, H., Utani, A., Endo, H.et al. (2003). The expression of nectin-1alpha in normal human skin and various skin tumours. Br. J. Dermatol., 148, 755–762.CrossRefGoogle ScholarPubMed
Mauri, D. N., Ebner, R., Montgomery, R. I.et al. (1998). LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are ligands for herpesvirus entry mediator. Immunity, 8, 21–30.CrossRefGoogle ScholarPubMed
McGeoch, D. J., Dalrymple, M. A., Davison, A. J.et al. (1988). The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J. Gen. Virol., 69, 1531–1574.CrossRefGoogle Scholar
Melancon, J. M., Foster, T. P., and Kousoulas, K. G. (2004). Genetic analysis of the herpes simplex virus type 1 UL20 protein domains involved in cytoplasmic virion envelopment and virus-induced cell fusion. J. Virol., 78, 7329–7343.CrossRefGoogle ScholarPubMed
Menotti, L., Lopez, M., Avitabile, E.et al. (2000). The murine homolog of human-Nectin1d serves as a species non-specific mediator for entry of human and animal aherpesviruses in a pathway independent of a detectable binding to gD. Proc. Natl Acad. Sci. USA, 97, 4867–4872.CrossRefGoogle Scholar
Menotti, L., Avitabile, E., Dubreuil, P., Lopez, M., and Campadelli-Fiume, G. (2001). Comparison of murine and human nectin1 binding to herpes simplex virus glycoprotein D (gD) reveals a weak interaction of murine nectin1 to gD and a gD-dependent pathway of entry. Virology, 282, 256–266.CrossRefGoogle Scholar
Menotti, L., Casadio, R., Bertucci, C., Lopez, M., and Campadelli-Fiume, G. (2002a). Substitution in the murine nectin1 receptor of a single conserved amino acid at a position distal from herpes simplex virus gD binding site confers high affinity binding to gD. J. Virol., 76, 5463–5471.CrossRefGoogle Scholar
Menotti, L., Cocchi, F., and Campadelli-Fiume, G. (2002b). Critical residues in the CC′ ridge of the human nectin1 receptor V domain enable herpes simplex virus entry into the cell and act synergistically with the downstream region. Virology, 301, 6–12.CrossRefGoogle Scholar
Milne, R. S., Connolly, S. A., Krummenacher, C., Eisenberg, R. J., and Cohen, G. H. (2001). Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a functional alphaherpesvirus receptor. Virology, 281, 315–328.CrossRefGoogle ScholarPubMed
Milne, R. S., Hanna, S. L., Rux, A. H., Willis, S. H., Cohen, G. H., and Eisenberg, R. J. (2003). Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusion. J. Virol., 77, 8962–8972.CrossRefGoogle ScholarPubMed
Mo, C., Lee, J., Sommer, M., Grose, C., and Arvin, A. M. (2002). The requirement of varicella zoster virus glycoprotein E (gE) for viral replication and effects of glycoprotein I on gE in melanoma cells. Virology, 304, 176–186.CrossRefGoogle ScholarPubMed
Montalvo, E. A. and Grose, C. (1986). Neutralization epitope of varicella zoster virus on native viral glycoprotein gp118 (VZV glycoprotein gpIII). Virology, 149, 230–241.CrossRefGoogle Scholar
Montgomery, R. I., Warner, M. S., Lum, B. J., and Spear, P. G. (1996). Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell, 87, 427–436.CrossRefGoogle ScholarPubMed
Nicola, A. V. and Straus, S. E. (2004). Cellular and viral requirements for rapid endocytic entry of herpes simplex virus. J. Virol., 78, 7508–7517.CrossRefGoogle ScholarPubMed
Nicola, A. V., Peng, C., Lou, H., Cohen, G. H., and Eisenberg, R. J. (1997). Antigenic structure of soluble herpes simplex virus (HSV) glycoprotein D correlates with inhibition of HSV infection. J. Virol., 71, 2940–2946.Google ScholarPubMed
Nicola, A. V., McEvoy, A. M., and Straus, S. E. (2003). Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J. Virol., 77, 5324–5332.CrossRefGoogle Scholar
Ojala, P. M., Sodeik, B., Ebersold, M. W., Kutay, U., and Helenius, A. (2000). Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol. Cell Biol., 20, 4922–4931.CrossRefGoogle ScholarPubMed
Olson, J. K. and Grose, C. (1997). Endocytosis and recycling of varicella-zoster virus Fc receptor glycoprotein gE: internalization mediated by a YXXL motif in the cytoplasmic tail. J. Virol., 71, 4042–4054.Google ScholarPubMed
Olson, J. K. and Grose, C. (1998). Complex formation facilitates endocytosis of the varicella-zoster virus gE:gI Fc receptor. J. Virol., 72, 1542–1551.Google ScholarPubMed
Olson, J. K., Santos, R. A., and Grose, C. (1998). Varicella-zoster virus glycoprotein gE: endocytosis and trafficking of the Fc receptor. J. Infect. Dis., 178 Suppl 1, S2–S6.CrossRefGoogle ScholarPubMed
Pasieka, T. J., Maresova, L., and Grose, C. (2003). A functional YNKI motif in the short cytoplasmic tail of varicella-zoster virus glycoprotein gH mediates clathrin-dependent and antibody-independent endocytosis. J. Virol., 77, 4191–4204.CrossRefGoogle ScholarPubMed
Pasieka, T. J., Maresova, L., Shiraki, K., and Grose, C. (2004). Regulation of varicella-zoster virus-induced cell-to-cell fusion by the endocytosis-competent glycoproteins gH and gE. J. Virol., 78, 2884–2896.CrossRefGoogle ScholarPubMed
Patera, A., Ali, M. A., Tyring, S.et al. (2002). Polymorphisms in the genes for herpesvirus entry. J. Infect. Dis., 186, 444–445.CrossRefGoogle ScholarPubMed
Pellett, P. E., Kousoulas, K. G., Pereira, L., and Roizman, B. (1985). Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: primary sequence and predicted protein structure of the wild type and of monoclonal antibody-resistant mutants. J. Virol., 53, 243–253.Google Scholar
Peng, T., Ponce de Leon, M., Novotny, M. J.et al. (1998). Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex. J. Virol., 72, 6092–6103.Google ScholarPubMed
Pereira, L., Ali, M., Kousoulas, K., Huo, B., and Banks, T. (1989). Domain structure of herpes simplex virus 1 glycoprotein B: neutralizing epitopes map in regions of continuous and discontinuous residues. Virology, 172, 11–24.CrossRefGoogle ScholarPubMed
Qadri, I., Gimeno, C., Navarro, D., and Pereira, L. (1991). Mutations in conformation-dependent domains of herpes simplex virus 1 glycoprotein B affect the antigenic properties, dimerization, and transport of the molecule. Virology, 180, 135–152.CrossRefGoogle ScholarPubMed
Reymond, N., Borg, J., Lecocq, E.et al. (2000). Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin. Gene, 255, 347–355.CrossRefGoogle ScholarPubMed
Richart, S., Simpson, S., Krummenacher, C.et al. (2003). Entry of herpes simplex virus type 1 into primary sensory neurons in vitro is mediated by Nectin-1/HveC. J. Virol., 77, 3307–3311.CrossRefGoogle ScholarPubMed
Roberts, S. R., Ponce de Leon, M., Cohen, G. H., and Eisenberg, R. J. (1991). Analysis of the intracellular maturation of the herpes simplex virus type 1 glycoprotein gH in infected and transfected cells. Virology, 184, 609–624.CrossRefGoogle ScholarPubMed
Roche, S., Bressanelli, S., Rey, F. A., and Gaudin, Y. (2006). Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science, 313, 187–191.CrossRefGoogle ScholarPubMed
Roop, C., Hutchinson, L., and Johnson, D. C. (1993). A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H. J. Virol., 67, 2285–2297.Google ScholarPubMed
Rux, A. H., Lou, H., Lambris, J. D., Friedman, H. M., Eisenberg, R. J., and Cohen, G. H. (2002). Kinetic analysis of glycoprotein C of herpes simplex virus types 1 and 2 binding to heparin, heparan sulfate, and complement component C3b. Virology, 294, 324–332.CrossRefGoogle ScholarPubMed
Santos, R. A., Padilla, J. A., Hatfield, C., and Grose, C. (1998). Antigenic variation of varicella zoster virus Fc receptor gE: loss of a major B cell epitope in the ectodomain. Virology, 249, 21–31.CrossRefGoogle Scholar
Santos, R. A., Hatfield, C. C., Cole, N. L.et al. (2000). Varicella-zoster virus gE escape mutant VZV-MSP exhibits an accelerated cell-to-cell spread phenotype in both infected cell cultures and SCID-hu mice. Virology, 275, 306–317.CrossRefGoogle ScholarPubMed
Schelhaas, M., Jansen, M., Haase, I., and Knebel-Morsdorf, D. (2003). Herpes simplex virus type 1 exhibits a tropism for basal entry in polarized epithelial cells. J. Gen. Virol., 84, 2473–2484.CrossRefGoogle ScholarPubMed
Shukla, D. and Spear, P. G. (2001). Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry. J. Clin. Invest., 108, 503–510.CrossRefGoogle ScholarPubMed
Shukla, D., Liu, J., Blaiklock, P.et al. (1999). A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell, 99, 13–22.CrossRefGoogle ScholarPubMed
Shukla, D.Canto, M. C., Rowe, C. L., and Spear, P. G. (2000). Striking Similarity of murine nectin-1alpha to human nectin-1alpha (HveC) in sequence and activity as a glycoprotein D receptor for alphaherpesvirus entry. J. Virol., 74, 11773–11781.CrossRefGoogle ScholarPubMed
Smith, G. A., Gross, S. P., and Enquist, L. W. (2001). Herpesviruses use bidirectional fast-axonal transport to spread in sensory neurons. Proc. Natl Acad. Sci. USA, 98, 3466–3470.CrossRefGoogle ScholarPubMed
Sodeik, B. (2000). Mechanisms of viral transport in the cytoplasm. Trends Microbiol, 8, 465–472.CrossRefGoogle ScholarPubMed
Sodeik, B., Ebersold, M. W., and Helenius, A. (1997). Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol., 136, 1007–1021.CrossRefGoogle ScholarPubMed
Spear, P. G., Shieh, M. T., Herold, B. C., WuDunn, D., and Koshy, T. I. (1992). Heparan sulfate glycosaminoglycans as primary cell surface receptors for herpes simplex virus. Adv. Exp. Med. Biol., 313, 341–353.CrossRefGoogle ScholarPubMed
Spear, P. G., Eisenberg, R. J., and Cohen, G. H. (2000). Three classes of cell surface receptors for alphaherpesvirus entry. Virology, 275, 1–8.CrossRefGoogle ScholarPubMed
Struyf, F., Posavad, C. M., Keyaerts, E., Ranst, M., Corey, L., and Spear, P. G. (2002). Search for polymorphisms in the genes for herpesvirus entry mediator, nectin-1, and nectin-2 in immune seronegative individuals. J. Infect. Dis., 185, 36–44.CrossRefGoogle ScholarPubMed
Takai, Y., Irie, K., Shimizu, K., Sakisaka, T., and Ikeda, W. (2003). Nectins and nectin-like molecules: roles in cell adhesion, migration, and polarization. Cancer Sci., 94, 655–667.CrossRefGoogle Scholar
Tal-Singer, R., Peng, C., Ponce De Leon, M.et al. (1995). Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface molecules. J. Virol., 69, 4471–4483.Google Scholar
Turner, A., Bruun, B., Minson, T., and Browne, H. (1998). Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system. J. Virol., 72, 873–875.Google Scholar
Ward, P. L., Campadelli-Fiume, G., Avitabile, E., and Roizman, B. (1994). Localization and putative function of the UL20 membrane protein in cells infected with herpes simplex virus 1. J. Virol., 68, 7406–7417.Google ScholarPubMed
Warner, M. S., Geraghty, R. J., Martinez, W. M.et al. (1998). A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus. Virology, 246, 179–189.CrossRefGoogle ScholarPubMed
Whitbeck, J. C., Muggeridge, M. I., Rux, A. H.et al. (1999). The major neutralizing antigenic site on herpes simplex virus glycoprotein D overlaps a receptor-binding domain. J. Virol., 73, 9879–9890.Google ScholarPubMed
Willis, S. H., Rux, A. H., Peng, C.et al. (1998). Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonance. J. Virol., 72, 5937–5947.Google ScholarPubMed
WuDunn, D. and Spear, P. G. (1989). Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J. Virol., 63, 52–58.Google ScholarPubMed
Yoon, M., Zago, A., Shukla, D., and Spear, P. G. (2003). Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, nectin-2, and 3-O-sulfated heparan sulfate but not with nectin-1. J. Virol., 77, 9221–9231.CrossRefGoogle Scholar
Zhou, G. and Roizman, B. (2006). Construction and properties of a herpes simplex virus 1 designed to enter cells solely via the IL-13alpha2 receptor. Proc. Natl Acad. Sci. USA, 103, 5508–5513.CrossRefGoogle ScholarPubMed
Zhou, G., Avitabile, E., Campadelli-Fiume, G., and Roizman, B. (2003). The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1. J. Virol., 77, 3759–3767.CrossRefGoogle ScholarPubMed

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