Mapping regions of Epstein-Barr virus (EBV) glycoprotein B (gB) important for fusion function with gH/gL

Virology

Volumn 413, Issue 1, 2011, Pages 26-38

  Plate, Aileen E ^a   Reimer, Jessica J ^a   Jardetzky, Theodore S ^b   Longnecker, Richard ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Epstein Barr virus; Fusion; Glycoprotein gB; Glycoprotein gH; Glycoprotein gL; Lymphocryptovirus; Rhesus

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN B; GLYCOPROTEIN H; HYBRID PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; B LYMPHOCYTE; CELL FUSION; CONTROLLED STUDY; EPSTEIN BARR VIRUS; FEMALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; VIRUS ENTRY;

AMINO ACID SEQUENCE; EPSTEIN-BARR VIRUS INFECTIONS; HERPESVIRUS 4, HUMAN; LYMPHOCRYPTOVIRUS; MEMBRANE GLYCOPROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; VIRAL ENVELOPE PROTEINS; VIRAL PROTEINS; VIRUS INTERNALIZATION;

CERCOPITHECINE HERPESVIRUS 15; HUMAN HERPESVIRUS 4; LYMPHOCRYPTOVIRUS; PRIMATES;

EID: 79953077970     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.12.006     Document Type: Article

References (54)

1. Atanasiu D., Whitbeck J.C., et al. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. Proc. Natl Acad. Sci. USA 2007, 104(47):18718-18723.
2. Atanasiu D., Whitbeck J.C., et al. Bimolecular complementation defines functional regions of HSV gB that are involved with gH/gL as necessary steps leading to cell fusion. J. Virol. 2010, 84(8):3825-3834.
3. Avitabile E., Forghieri C., et al. Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein. J. Virol. 2007, 81(20):11532-11537.
4. Avitabile E., Forghieri C., et al. Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD. J. Virol. 2009, 83(20):10752-10760.
5. Babcock G.J., Decker L.L., et al. EBV persistence in memory B cells in vivo. Immunity 1998, 9(3):395-404.
6. Backovic M., Jardetzky T.S. Class III viral membrane fusion proteins. Curr. Opin. Struct. Biol. 2009, 19(2):189-196.
7. Backovic M., Jardetzky T.S., et al. Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity. J. Virol. 2007, 81(17):9596-9600.
8. Backovic M., Longnecker R., et al. Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B. Proc. Natl Acad. Sci. USA 2009, 106(8):2880-2885.
9. Balachandran N., Oba D.E., et al. Antigenic cross-reactions among herpes simplex virus types 1 and 2, Epstein-Barr virus, and cytomegalovirus. J. Virol. 1987, 61(4):1125-1135.
10. Chesnokova L.S., Nishimura S.L., et al. Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8. Proc. Natl Acad. Sci. USA 2009, 106(48):20464-20469.
11. Cho Y.G., Gordadze A.V., et al. Evolution of two types of rhesus lymphocryptovirus similar to type 1 and type 2 Epstein-Barr virus. J. Virol. 1999, 73(11):9206-9212.
12. Chowdary T.K., Cairns T.M., et al. Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL. Nat. Struct. Mol. Biol. 2010, 17(7):882-889.
13. Claesson-Welsh L., Spear P.G. Oligomerization of herpes simplex virus glycoprotein B. J. Virol. 1986, 60(2):803-806.
14. Emini E.A., Luka J., et al. Identification of an Epstein-Barr virus glycoprotein which is antigenically homologous to the varicella-zoster virus glycoprotein II and the herpes simplex virus glycoprotein B. Virology 1987, 157(2):552-555.
15. Fingeroth J.D., Weis J.J., et al. Epstein-Barr virus receptor of human B lymphocytes is the C3d receptor CR2. Proc. Natl Acad. Sci. USA 1984, 81(14):4510-4514.
16. Gong M., Kieff E. Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. J. Virol. 1990, 64(4):1507-1516.
17. Gong M., Ooka T., et al. Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J. Virol. 1987, 61(2):499-508.
18. Grunewald K., Desai P., et al. Three-dimensional structure of herpes simplex virus from cryo-electron tomography. Science 2003, 302(5649):1396-1398.
19. Haan K.M., Lee S.K., et al. Different functional domains in the cytoplasmic tail of glycoprotein B are involved in Epstein-Barr virus-induced membrane fusion. Virology 2001, 290(1):106-114.
20. Hannah B.P., Heldwein E.E., et al. Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B. J. Virol. 2007, 81(9):4858-4865.
21. Hannah B.P., Cairns T.M., et al. Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops. J. Virol. 2009, 83(13):6825-6836.
22. Heldwein E.E., Lou H., et al. Crystal structure of glycoprotein B from herpes simplex virus 1. Science 2006, 313(5784):217-220.
23. Hutchinson L., Browne H., et al. 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. 1992, 66(4):2240-2250.
24. Kerppola T.K. Complementary methods for studies of protein interactions in living cells. Nat. Methods 2006, 3(12):969-971.
25. Kerppola T.K. Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat. Protoc. 2006, 1(3):1278-1286.
26. Kerppola T.K. Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 2006, 7(6):449-456.
27. Kirschner A.N., Omerovic J., et al. Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion. J. Virol. 2006, 80(19):9444-9454.
28. Lee S.K. Four consecutive arginine residues at positions 836-839 of EBV gp110 determine intracellular localization of gp110. Virology 1999, 264(2):350-358.
29. Li Q., Turk S.M., et al. The Epstein-Barr virus (EBV) BZLF2 gene product associates with the gH and gL homologs of EBV and carries an epitope critical to infection of B cells but not of epithelial cells. J. Virol. 1995, 69(7):3987-3994.
30. Li Q., Spriggs M.K., et al. Epstein-Barr virus uses HLA class II as a cofactor for infection of B lymphocytes. J. Virol. 1997, 71(6):4657-4662.
31. McShane M.P., Longnecker R. Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins. Proc. Natl Acad. Sci. USA 2004, 101(50):17474-17479.
32. Moghaddam A., Koch J., et al. Infection of human B lymphocytes with lymphocryptoviruses related to Epstein-Barr virus. J. Virol. 1998, 72(4):3205-3212.
33. Nagai T., Ibata K., et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20(1):87-90.
34. Nemerow G.R., Wolfert R., et al. Identification and characterization of the Epstein-Barr virus receptor on human B lymphocytes and its relationship to the C3d complement receptor (CR2). J. Virol. 1985, 55(2):347-351.
35. Neuhierl B., Feederle R., et al. Glycoprotein gp110 of Epstein-Barr virus determines viral tropism and efficiency of infection. Proc. Natl Acad. Sci. USA 2002, 99(23):15036-15041.
36. Okuma K., Nakamura M., et al. Host range of human T-cell leukemia virus type I analyzed by a cell fusion-dependent reporter gene activation assay. Virology 1999, 254(2):235-244.
37. Omerovic J., Longnecker R. Functional homology of gHs and gLs from EBV-related gamma-herpesviruses for EBV-induced membrane fusion. Virology 2007, 365(1):157-165.
38. Omerovic J., Lev L., et al. The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells. J. Virol. 2005, 79(19):12408-12415.
39. Papworth M.A., Van Dijk A.A., et al. The processing, transport and heterologous expression of Epstein-Barr virus gp110. J. Gen. Virol. 1997, 78(Pt 9):2179-2189.
40. Plate A.E., Smajlovic J., et al. Functional analysis of glycoprotein L (gL) from rhesus lymphocryptovirus in Epstein-Barr virus-mediated cell fusion indicates a direct role of gL in gB-induced membrane fusion. J. Virol. 2009, 83(15):7678-7689.
41. Reimer J.J., Backovic M., et al. Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis. J. Virol. 2009, 83(2):734-747.
42. Epstein-Barr virus. Fields Virology 2007, Lippincott Williams & Wilkins, Philadelphia, PA. A. Rickinson (Ed.).
43. Rivailler P., Cho Y.G., et al. Complete genomic sequence of an Epstein-Barr virus-related herpesvirus naturally infecting a new world primate: a defining point in the evolution of oncogenic lymphocryptoviruses. J. Virol. 2002, 76(23):12055-12068.
44. Rivailler P., Jiang H., et al. Complete nucleotide sequence of the rhesus lymphocryptovirus: genetic validation for an Epstein-Barr virus animal model. J. Virol. 2002, 76(1):421-426.
45. Rivailler P., Carville A., et al. Experimental rhesus lymphocryptovirus infection in immunosuppressed macaques: an animal model for Epstein-Barr virus pathogenesis in the immunosuppressed host. Blood 2004, 104(5):1482-1489.
46. Roche S., Bressanelli S., et al. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 2006, 313(5784):187-191.
47. Silva A.L., Omerovic J., et al. Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusion. J. Virol. 2004, 78(11):5946-5956.
48. Sorem J., Longnecker R. Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells. J. Gen. Virol. 2009, 90(Pt 3):591-595.
49. Spear P.G., Longnecker R. Herpesvirus entry: an update. J. Virol. 2003, 77(19):10179-10185.
50. Speck P., Haan K.M., et al. Epstein-Barr virus entry into cells. Virology 2000, 277(1):1-5.
51. Tanner J., Weis J., et al. Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis. Cell 1987, 50(2):203-213.
52. Thorley-Lawson D.A., Babcock G.J. A model for persistent infection with Epstein-Barr virus: the stealth virus of human B cells. Life Sci. 1999, 65(14):1433-1453.
53. Wang F., Rivailler P., et al. Simian homologues of Epstein-Barr virus. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2001, 356(1408):489-497.
54. Wu L., Hutt-Fletcher L.M. Compatibility of the gH homologues of Epstein-Barr virus and related lymphocryptoviruses. J. Gen. Virol. 2007, 88(Pt 8):2129-2136.