Mutations in the amino terminus of herpes simplex virus type 1 gL can reduce cell-cell fusion without affecting gH/gL trafficking

Journal of Virology

Volumn 88, Issue 1, 2014, Pages 739-744

  Zhou, Wenbo ^a   Chen, Feng ^a,c   Klyachkin, Yuri ^b   Sham, Yuk Y ^a   Geraghty, Robert J ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

^c PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; HETERODIMER; NECTIN 1;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL FUSION; CELL MIGRATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DELETION MUTANT; FEMALE; GENE DELETION; HERPES SIMPLEX VIRUS 1; IMMUNOPRECIPITATION; MEMBRANE FUSION; MUTAGENESIS; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; SEQUENCE ANALYSIS; VIRUS MUTATION;

AMINO ACID SEQUENCE; CELL FUSION; HERPESVIRUS 1, HUMAN; MOLECULAR SEQUENCE DATA; MUTATION; VIRAL PROTEINS;

EID: 84890863763     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02383-13     Document Type: Article

References (30)

1. Muggeridge MI. 2000. Characterization of cell-cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells. J. Gen. Virol. 81:2017-2027. http://vir.sgmjournals.org/content/81/8/201 7.long.
2. Pertel PE, Fridberg A, Parish ML, Spear PG. 2001. Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate. Virology 279:313-324. http: //dx.doi.org/10.1006/viro.2000.0713.
3. Turner A, Bruun B, Minson T, 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.
4. Dubin G, Jiang H. 1995. Expression of herpes simplex virus type 1 glycoprotein L (gL) in transfected mammalian cells: evidence that gL is not independently anchored to cell membranes. J. Virol. 69:4564-4568.
5. Hutchinson L, Browne H, Wargent V, Davis-Poynter N, Primorac S, Goldsmith K, Minson AC, Johnson DC. 1992. A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoproteinH(gH) and affects normal folding and surface expression of gH. J. Virol. 66:2240-2250.
6. Browne H, Bell S, Minson T, Wilson DW. 1996. An endoplasmic reticulumretained herpes simplex virus glycoproteinHis absent from secreted virions: evidence for reenvelopment during egress. J. Virol. 70:4311-4316.
7. Klyachkin YM, Stoops KD, Geraghty RJ. 2006. Herpes simplex virus type 1 glycoprotein L mutants that fail to promote trafficking of glycoproteinH and fail to function in fusion can induce binding of glycoprotein L-dependent anti-glycoprotein H antibodies. J. Gen. Virol. 87:759-767. http://vir .sgmjournals.org/content/87/4/759.long.
8. Galdiero S, Falanga A, Vitiello M, Browne H, Pedone C, Galdiero M. 2005. Fusogenic domains in herpes simplex virus type 1 glycoprotein H. J. Biol. Chem. 280:28632-28643. http://dx.doi.org/10.1074/jbc.M505196200.
9. Galdiero S, Falanga A, Vitiello M, D'Isanto M, Collins C, Orrei V, Browne H, Pedone C, Galdiero M. 2007. Evidence for a role of the membrane-proximal region of herpes simplex virus type 1 glycoproteinH in membrane fusion and virus inhibition. Chembiochem 8:885-895. http: //dx.doi.org/10.1002/cbic.200700044.
10. Gianni T, Martelli PL, Casadio R, Campadelli-Fiume G. 2005. The ectodomain of herpes simplex virus glycoprotein H contains a membrane α-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family. J. Virol. 79:2931-2940. http://dx.doi .org/10.1128/JVI.79.5.2931-2940.2005.
11. Gianni T, Menotti L, Campadelli-Fiume G. 2005. A heptad repeat in herpes simplex virus 1 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. http://dx.doi.org/10.1128/JVI.79.11.7042-7049.2005.
12. Gianni T, Piccoli A, Bertucci C, Campadelli-Fiume G. 2006. 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. http://dx.doi .org/10.1128/JVI.80.5.2216-2224.2006.
13. Subramanian RP, Geraghty RJ. 2007. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B. Proc. Natl. Acad. Sci. U. S. A. 104:2903-2908. http://dx.doi.org/10.1073/pnas.0608374104.
14. Atanasiu D, Cairns TM, Whitbeck JC, Saw WT, Rao S, Eisenberg RJ, Cohen GH. 2013. Regulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors. mBio 4(2):e00046 -13. http://dx.doi.org/10.1128/mBio.00046-13.
15. Atanasiu D, Saw WT, Cohen GH, Eisenberg RJ. 2010. Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB. J. Virol. 84:12292-12299. http://dx.doi.org/10.1128 /JVI.01700-10.
16. Chowdary TK, Cairns TM, Atanasiu D, Cohen GH, Eisenberg RJ, Heldwein EE. 2010. Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL. Nat. Struct. Mol. Biol. 17:882-888. http://dx .doi.org/10.1038/nsmb.1837.
17. Jackson JO, Longnecker R. 2010. Reevaluating herpes simplex virus hemifusion. J. Virol. 84:11814-11821. http://dx.doi.org/10.1128/JVI .01615-10.
18. Klyachkin YM, Geraghty RJ. 2008. Mutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function. Virology 374:23-32. http://dx.doi.org/10.1016/j.virol.2007.11 .014.
19. Peng T, Ponce de Leon M, Novotny MJ, Jiang H, Lambris JD, Dubin G, Spear PG, Cohen GH, Eisenberg RJ. 1998. Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex. J. Virol. 72:6092-6103.
20. Novotny MJ, Parish ML, Spear PG. 1996. Variability of herpes simplex virus 1 gL and anti-gL antibodies that inhibit cell fusion but not viral infectivity. Virology 221:1-13. http://dx.doi.org/10.1006/viro.1996.0347.
21. Fan Q, Lin E, Spear PG. 2009. Insertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion. J. Virol. 83:11607-11615. http://dx.doi.org/10.1128 /JVI.01369-09.
22. Gompels UA, Minson AC. 1986. The properties and sequence of glycoproteinHof herpes simplex virus type 1. Virology 153:230-247. http://dx .doi.org/10.1016/0042-6822(86)90026-7.
23. Gompels UA, Minson AC. 1989. Antigenic properties and cellular localization of herpes simplex virus glycoprotein H synthesized in a mammalian cell expression system. J. Virol. 63:4744-4755.
24. Tang J, Maddali K, Pommier Y, Sham YY, Wang Z. 2010. Scaffold rearrangement of dihydroxypyrimidine inhibitors of HIV integrase: docking model revisited. Bioorg. Med. Chem. Lett. 20:3275-3279. http://dx .doi.org/10.1016/j.bmcl.2010.04.048.
25. Zhang Y, Sham YY, Rajamani R, Gao J, Portoghese PS. 2005. Homology modeling and molecular dynamics simulations of the mu opioid receptor in a membrane-aqueous system. Chembiochem 6:853-859. http://dx.doi .org/10.1002/cbic.200400207.
26. Jorgensen WL, Maxwell DS, Tirado-Rives J. 1996. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236.
27. Ghosh A, Rapp CS, Friesner RA. 1998. Generalized Born model based on a surface integral formulation. J. Phys. Chem. B 102:10983-10990.
28. Roop C, Hutchinson L, Johnson DC. 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.
29. Cairns TM, Friedman LS, Lou H, Whitbeck JC, Shaner MS, Cohen GH, Eisenberg RJ. 2007. N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for function. J. Virol. 81:5102- 5111. http://dx.doi.org/10.1128/JVI.00097-07.
30. Cairns TM, Shaner MS, Zuo Y, Ponce-de-Leon M, Baribaud I, Eisenberg RJ, Cohen GH, Whitbeck JC. 2006. Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function. J. Virol. 80:2596-2608. http://dx.doi .org/10.1128/JVI.80.6.2596-2608.2006.