Cell-based analysis of Chikungunya virus membrane fusion using baculovirus-expression vectors

Journal of Virological Methods

Volumn 175, Issue 2, 2011, Pages 206-215

  Kuo, Szu Cheng ^a,b   Chen, Ying Ju ^c   Wang, Yu Ming ^b   Kuo, Ming Der ^b   Jinn, Tzyy Rong ^d   Chen, Wen Shuo ^e   Chang, Yen Chung ^e   Tung, Kuo Lun ^c   Wu, Tzong Yuan ^c   Lo, Szecheng J ^a  

^a CHANG GUNG UNIVERSITY   (Taiwan)

^b NATIONAL DEFENSE MEDICAL CENTER   (Taiwan)

^c CHUNG YUAN CHRISTIAN UNIVERSITY   (Taiwan)

^d CHINA MEDICAL UNIVERSITY   (Taiwan)

^e NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

Baculovirus; Chikungunya virus; Internal ribosome entry site; Syncytium; Viral membrane fusion

Indexed keywords

CAPSID PROTEIN; CHOLESTEROL; ENHANCED GREEN FLUORESCENT PROTEIN; GLYCOPROTEIN E1; GLYCOPROTEIN E2; STRUCTURAL PROTEIN;

ARTICLE; BACULOVIRUS EXPRESSION SYSTEM; CELL ASSAY; CELL FUSION; CELL SURFACE; CHIKUNGUNYA ALPHAVIRUS; CISTRON; CONTROLLED STUDY; INSECT CELL; LEPIDOPTERA; MEMBRANE FUSION; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; SYNCYTIUM; WESTERN BLOTTING;

ANIMALS; BACULOVIRIDAE; CELL CULTURE TECHNIQUES; CELL FUSION; CELL LINE; CHIKUNGUNYA VIRUS; GENE EXPRESSION; GENES, REPORTER; GREEN FLUORESCENT PROTEINS; RECOMBINANT FUSION PROTEINS; SPODOPTERA; VIRAL STRUCTURAL PROTEINS; VIRUS INTERNALIZATION;

ALPHAVIRUS; CHIKUNGUNYA VIRUS; HEXAPODA; MIRIDAE; SPODOPTERA FRUGIPERDA;

EID: 79959340043     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2011.05.015     Document Type: Article

References (48)

1. Bernard E., Solignat M., Gay B., Chazal N., Higgs S., Devaux C., Briant L. Endocytosis of Chikungunya virus into mammalian cells: role of clathrin and early endosomal compartments. PLoS One 2010, 5:e11479.
2. Blissard G.W., Wenz J.R. Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-dependent membrane fusion. J. Virol. 1992, 66:6829-6835.
3. Boggs W.M., Hahn C.S., Strauss E.G., Strauss J.H., Griffin D.E. Low pH-dependent Sindbis virus-induced fusion of BHK cells: differences between strains correlate with amino acid changes in the E1 glycoprotein. Virology 1989, 169:485-488.
4. Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal. Biochem. 1976, 72:248-254.
5. Bressanelli S., Stiasny K., Allison S.L., Stura E.A., Duquerroy S., Lescar J., Heinz F.X., Rey F.A. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 2004, 23:728-738.
6. Chanel-Vos C., Kielian M. A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion. J. Virol. 2004, 78:13543-13552.
7. Chatterjee P.K., Vashishtha M., Kielian M. Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion. J. Virol. 2000, 74:1623-1631.
8. Chen Y.J., Chen W.S., Wu T.Y. Development of a bi-cistronic baculovirus expression vector by the Rhopalosiphum padi virus 5' internal ribosome entry site. Biochem. Biophys. Res. Commun. 2005, 335:616-623.
9. Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B., Lepault J., Kielian M., Rey F.A. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 2004, 427:320-325.
10. Gollins S.W., Porterfield J.S. A new mechanism for the neutralization of enveloped viruses by antiviral antibody. Nature 1986, 321:244-246.
11. Grace T.D. Establishment of four strains of cells from insect tissues grown in vitro. Nature 1962, 195:788-789.
12. Harrison S.C. Viral membrane fusion. Nat. Struct. Mol. Biol. 2008, 15:690-698.
13. Kempf C., Michel M.R., Kohler U., Koblet H. A novel method for the detection of early events in cell-cell fusion of Semliki Forest virus infected cells growing in monolayer cultures. Arch. Virol. 1987, 95:283-289.
14. Kielian M., Jungerwirth S., Sayad K.U., DeCandido S. Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein. J. Virol. 1990, 64:4614-4624.
15. Kielian M., Klimjack M.R., Ghosh S., Duffus W.A. Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus. J. Cell Biol. 1996, 134:863-872.
16. Kielian M., Rey F.A. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 2006, 4:67-76.
17. Kielian M.C., Helenius A. Role of cholesterol in fusion of Semliki Forest virus with membranes. J. Virol. 1984, 52:281-283.
18. Kilby J.M., Eron J.J. Novel therapies based on mechanisms of HIV-1 cell entry. N. Engl. J. Med. 2003, 348:2228-2238.
19. Klimjack M.R., Jeffrey S., Kielian M. Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein. J. Virol. 1994, 68:6940-6946.
20. Lanzrein M., Kasermann N., Weingart R., Kempf C. Early events of Semliki Forest virus-induced cell-cell fusion. Virology 1993, 196:541-547.
21. Laras K., Sukri N.C., Larasati R.P., Bangs M.J., Kosim R., Djauzi, Wandra T., Master J., Kosasih H., Hartati S., Beckett C., Sedyaningsih E.R., Beecham H.J., Corwin A.L. Tracking the re-emergence of epidemic Chikungunya virus in Indonesia. Trans. R. Soc. Trop. Med. Hyg. 2005, 99:128-141.
22. Li L., Jose J., Xiang Y., Kuhn R.J., Rossmann M.G. Structural changes of envelope proteins during alphavirus fusion. Nature 2010, 468:705-708.
23. Liljestrom P., Garoff H. Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor. J. Virol. 1991, 65:147-154.
24. Mackenzie J.S., Chua K.B., Daniels P.W., Eaton B.T., Field H.E., Hall R.A., Halpin K., Johansen C.A., Kirkland P.D., Lam S.K., McMinn P., Nisbet D.J., Paru R., Pyke A.T., Ritchie S.A., Siba P., Smith D.W., Smith G.A., van den Hurk A.F., Wang L.F., Williams D.T. Emerging viral diseases of Southeast Asia and the Western Pacific. Emerg. Infect. Dis. 2001, 7:497-504.
25. Melancon P., Garoff H. Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease. J. Virol. 1987, 61:1301-1309.
26. Nybakken G.E., Oliphant T., Johnson S., Burke S., Diamond M.S., Fremont D.H. Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 2005, 437:764-769.
27. O'Reilly D.R., Luckow M.L.K.V.A. Baculovirus Expression Vector: A Laboratory Manual 1992, W.H. Freeman and Co., NY.
28. Omar A., Koblet H. Semliki Forest virus particles containing only the E1 envelope glycoprotein are infectious and can induce cell-cell fusion. Virology 1988, 166:17-23.
29. Ozden S., Lucas-Hourani M., Ceccaldi P.E., Basak A., Valentine M., Benjannet S., Hamelin J., Jacob Y., Mamchaoui K., Mouly V., Despres P., Gessain A., Butler-Browne G., Chretien M., Tangy F., Vidalain P.O., Seidah N.G. Inhibition of Chikungunya virus infection in cultured human muscle cells by furin inhibitors: impairment of the maturation of the E2 surface glycoprotein. J. Biol. Chem. 2008, 283:21899-21908.
30. Pastorino B., Muyembe-Tamfum J.J., Bessaud M., Tock F., Tolou H., Durand J.P., Peyrefitte C.N. Epidemic resurgence of Chikungunya virus in democratic Republic of the Congo: identification of a new central African strain. J. Med. Virol. 2004, 74:277-282.
31. Randolph V.B., Stollar V. Low pH-induced cell fusion in flavivirus-infected Aedes albopictus cell cultures. J. Gen. Virol. 1990, 71:1845-1850.
32. Reeda H.M. A simple method for estimating fifty percent endpoints. Am. J. Hyg. 1938, 27:5.
33. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning-A Laboratory Manual 1989, Cold Spring Harbor Laboratory Press, NY. 2nd ed.
34. Sanchez-San Martin C., Liu C.Y., Kielian M. Dealing with low pH: entry and exit of alphaviruses and flaviviruses. Trends Microbiol. 2009, 17:514-521.
35. Sanz M.A., Rejas M.T., Carrasco L. Individual expression of sindbis virus glycoproteins, E1 alone promotes cell fusion. Virology 2003, 305:463-472.
36. Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 2000, 69:531-569.
37. Smit J.M., Bittman R., Wilschut J. Low-pH-dependent fusion of Sindbis virus with receptor-free cholesterol- and sphingolipid-containing liposomes. J. Virol. 1999, 73:8476-8484.
38. Solignat M., Gay B., Higgs S., Briant L., Devaux C. Replication cycle of Chikungunya: a re-emerging arbovirus. Virology 2009, 393:183-197.
39. Strauss J.H., Strauss E.G. The alphaviruses: gene expression, replication, and evolution. Microbiol. Rev. 1994, 58:491-562.
40. Thaikruea L., Charearnsook O., Reanphumkarnkit S., Dissomboon P., Phonjan R., Ratchbud S., Kounsang Y., Buranapiyawong D. Chikungunya in Thailand: a re-emerging disease?. Southeast Asian J. Trop. Med. Public Health 1997, 28:359-364.
41. Voss J.E., Vaney M.C., Duquerroy S., Vonrhein C., Girard-Blanc C., Crublet E., Thompson A., Bricogne G., Rey F.A. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 2010, 468:709-712.
42. Wahlberg J.M., Bron R., Wilschut J., Garoff H. Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J. Virol. 1992, 66:7309-7318.
43. Wahlberg J.M., Garoff H. Membrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells. J. Cell Biol. 1992, 116:339-348.
44. White J., Helenius A. pH-dependent fusion between the Semliki Forest virus membrane and liposomes. Proc. Natl. Acad. Sci. U.S.A. 1980, 77:3273-3277.
45. Wu T.Y., Liono L., Chen S.L., Chen C.Y., Chao Y.C. Expression of highly controllable genes in insect cells using a modified tetracycline-regulated gene expression system. J. Biotechnol. 2000, 80:75-83.
46. Yergolkar P.N., Tandale B.V., Arankalle V.A., Sathe P.S., Sudeep A.B., Gandhe S.S., Gokhle M.D., Jacob G.P., Hundekar S.L., Mishra A.C. Chikungunya outbreaks caused by African genotype, India. Emerg. Infect. Dis. 2006, 12:1580-1583.
47. Zhang X., Fugere M., Day R., Kielian M. Furin processing and proteolytic activation of Semliki Forest virus. J. Virol. 2003, 77:2981-2989.
48. Zwick M.B. The membrane-proximal external region of HIV-1 gp41: a vaccine target worth exploring. AIDS 2005, 19:1725-1737.