Structural basis for paramyxovirus-mediated membrane fusion

Molecular Cell

Volumn 3, Issue 3, 1999, Pages 309-319

  Baker, Kent A ^a   Dutch, Rebecca Ellis ^a   Lamb, Robert A ^a,b   Jardetzky, Theodore S ^a  

^a Department of Biochemistry ^*  (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS FUSION PROTEIN;

ARTICLE; BILAYER MEMBRANE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DELETION MUTANT; MEMBRANE FUSION; MEMBRANE STRUCTURE; NONHUMAN; PARAINFLUENZA VIRUS; PARAMYXOVIRUS; PROTEIN DOMAIN; VIRUS CELL INTERACTION; VIRUS ENVELOPE;

EID: 0033106334     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80458-X     Document Type: Article

References (45)

1. Bagai, S., and Lamb, R.A. (1995). Quantitative measurement of paramyxovirus fusion: Differences in requirements of glycoproteins between simian virus 5 and human parainfluenza virus 3 or Newcastle disease virus. J. Virol. 69, 6712-6719.
2. Blacklow, S.C., Lu, M., and Kim, P.S. (1995). Atrimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 34, 14956-14962.
3. Brown, J.H., Cohen, C., and Parry, D.A. (1996). Heptad breaks on α-helical coiled coils: Stutters and stammers. Proteins 26, 134-145.
4. Brünger, AT., Adams, P.D., Clore, G.M., Gros, P., Grosse-Kuntsleve, R.W., Jiang, J.-S., Kuszerski, J., Pannu, N.S., and Read, R.J. (1998). Crystallographic and NMR system (CNS): A new software system for macromolecular structure determination. Acta Crystallogr. D 54, 905-921.
5. Bullough, P.A., Hughson, F.M., Skehel, J.J., and Wiley, D.C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43.
6. Caffrey, M., Cai, M., Kaufman, J., Stahl, S.J., Gronenborn, A.M., and Clore, G.M. (1998). Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J. 177, 4572-4584.
7. Carr, C.M., and Kim, P.S. (1993). A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832.
8. Chambers, P., Pringle, C.R., and Easton, A.J. (1990). Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71, 3075-3080.
9. Chan, D.C., and Kim, P.S. (1998). HIV entry and its inhibition. Cell 93, 681-684.
10. Chan, D.C., Fass, D., Berger, J.M., and Kim, P.S. (1997). Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273.
11. Chen, J., Wharton, S.A., Weissenhorn, W., Calder, L.J., Hughson, F.M., Skehel, J.J., and Wiley, D.C. (1995). A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Natl. Acad. Sci. USA 92, 12205-12209.
12. Chen, J., Lee, K.H., Steinhauer, D.A., Stevens, D.J., Skehel, J.J., and Wiley, D.C. (1998). Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95, 409-417.
13. Collaborative Computational Project, No. 4 (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50, 760-763.
14. Collins, P.L., Chanock, R.M., and Mclntosh, K. (1996). Parainfluenza viruses. In Fields Virology, Third Edition, B.N. Fields, D.M. Knipe, and P.M. Howley, eds. (Philadelphia: Lippincott-Raven Publishers), pp. 1205-1241.
15. Damico, R.L., Crane, J., and Bates, P. (1998). Receptor-triggered membrane association of a model retroviral glycoprotein. Proc. Natl. Acad. Sci. USA 95, 2580-2585.
16. De La Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. in Methods in Enzymology: Macromolecular Crystallography, R.M. Sweet and C.W. Carter, eds. (New York: Academic Press), pp. 472-494.
17. Dutch, R.E., Leser, G.P., and Lamb, R.A. (1999). Paramyxovirus fusion protein: Characterization of the core trimer, a rod-shaped complex with helices in anti-parallel orientation. Virology 254, 147-159.
18. Fass, D., and Kim, P.S. (1995). Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr. Biol. 5, 1377-1383.
19. Fass, D., Harrison, S.C., and Kim, P.S. (1996). Retrovirus envelope domain at 1.7 Å resolution. Nat. Struct. Biol. 3, 465-469.
20. Furuta, R.A., Wild, C.T., Weng, Y., and Weiss, C.D. (1998). Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5, 276-279.
21. Hernandez, L.D., Huffman, L.R., Wolfsberg, T.G., and White, J.M. (1996). Virus-cell and cell-cell fusion. Annu. Rev. Cell Dev. Biol. 12, 627-661.
22. Hernandez, L.D., Peters, R.J., Delos, S.E., Young, J.A.T., Agard, D.A., and White, J.M. (1997). Activation of a retroviral membrane fusion protein: Soluble receptor-induced liposome binding of the ALSV envelope glycoprotein. J. Cell Biol. 139, 1455-1464.
23. Horvath, C.M., and Lamb, R.A. (1992). Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: Roles of conserved residues in cell fusion. J. Virol. 66, 2443-2455.
24. Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
25. Joshi, S.B., Dutch, R.E., and Lamb, R.A. (1998). A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 248, 20-34.
26. Lamb, R.A. (1993). Paramyxovirus fusion: A hypothesis for changes. Virology 197, 1-11.
27. Lamb, R.A., and Kolakofsky, D. (1996). Paramyxoviridae: The viruses and their replication. In Fields Virology, Third Edition, B.N. Fields, D.M. Knipe, and P.M. Howley, eds. (Philadelphia: Lippincott-Raven Publishers), pp. 1177-1204.
28. Lu, M., Blacklow, S.C., and Kim, P.S. (1995). A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2, 1075-1082.
29. Mackenzie, K.R., and Engelman, D.M. (1998). Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization. Proc. Natl. Acad. Sci. USA 95, 3583-3590.
30. Mackenzie, K.R., Prestegard, J.H., and Engelman, D.M. (1997). A transmembrane helix dimer: Structure and implications. Science 276, 131-133.
31. Malashkevich, V.N., Chan, D.C., Chutkowski, C.T., and Kirn, P.S. (1998). Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl. Acad. Sci. USA 95, 9134-9139.
32. Moore, J.P., McKeating, J.A., Weiss, R.A., and Sattentau, Q.J. (1990). Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250, 1130-1142.
33. Morrison, T., and Portner, A. (1991). Structure, function, and intracellular processing of the glycoproteins of paramyxoviridae. In The Paramyxoviruses, D.W. Kingsbury, ed. (New York: Plenum Press), pp. 347-382.
34. Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
35. Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology: MacRomolecular Crystallography, Part A, R.M. Sweet and C.W. Carter, eds. (New York: Academic Press), pp. 307-326.
36. Rapaport, D., Ovadia, M., and Shai, Y. (1995). A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of sendai virus-cell fusion: An emerging similarity with functional domains of other viruses. EMBO J. 14, 5524-5531.
37. Rosenthal, P.B., Zhang, X., Formanowski, F., Fitz, W., Wong, C.-H., Meier-Ewert, H., Skehel, J.J., and Wiley, D.C. (1998). Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus. Nature 396, 92-96.
38. Ruigrok, R.W.H., Martin, S.R., Wharton, S.A., Skehel, J.J., Bayley, P.M., and Wiley, D.C. (1986). Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes. Virology 155, 484-497.
39. Tan, K., Liu, J.-H., Wang, J.-H., Shen, S., and Lu, M. (1997). Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94, 12303-12308.
40. Weissenhorn, W., Wharton, S.A., Calder, L.J., Earl, P.L., Moss, B., Aliprandis, E., Skehel, J.J., and Wiley, D.C. (1996). The ectodomain of HIV-1 env subunit gp41 forms a soluble, a-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 15, 1507-1514.
41. Weissenhorn, W., Dessen, A., Harrison, S.C., Skehel, J.J., and Wiley, D.C. (1997). Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426-430.
42. Weissenhorn, W., Calder, L.J., Wharton, S.A., Skehel, J.J., and Wiley, D.C. (1998a). The central structural feature of the membrane fusion protein subunit from the ebola virus glycoprotein is a long triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA 95, 6032-6036.
43. Weissenhorn, W., Carfi, A., Lee, K.-H., Skehel, J.J., and Wiley, D.C. (1998b). Crystal structure of the ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell 2, 605-616.
44. Wilson, I.A., Skehel, J.J., and Wiley, D.C. (1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-375.
45. Zhou, J., Dutch, R.E., and Lamb, R.A. (1997). Proper spacing between heptad repeat B and the transmembrane domain boundary of the paramyxovirus SV5 F protein is critical for biological activity. Virology 239, 327-339.