Alphavirus Structure

  • Stephen C. Harrison
Part of the The Viruses book series (VIRS)


Alphavirus particles are roughly spherical, with three principal substructures—an outer glycoprotein shell, a lipid bilayer, and an RNA-containing core (nucleocapsid). The radial organization of these components is summarized in Fig. 1. The most extensive structural studies have been carried out on Sindbis virus and Semliki Forest virus (SFV). It is on these very similar viruses that the description below will focus.


Influenza Virus Lipid Bilayer Transmembrane Segment Semliki Forest Virus Sindbis Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Adrian, M., Dubochet, J., Lepault, J., and McDowell, A. W., 1984, Cryo-electron microscopy of viruses, Nature (London) 308: 32–36.CrossRefGoogle Scholar
  2. Gahmberg, C. G., Utermann, G., and Simons, K., 1972, The membrane proteins of Semliki Forest virus have a hydrophobic part attached to the viral membrane, FEBS Lett. 28: 179–182.CrossRefGoogle Scholar
  3. Garoff, H., and Simons, K., 1974, Location of the spike glycoproteins in the Semliki Forest virus membrane, Proc. Natl. Acad. Sci. U.S.A. 71: 3988–3992.PubMedCrossRefGoogle Scholar
  4. Garoff, H., and Söderlund, H., 1978, The amphiphobic membrane glycoproteins of Semliki Forest virus are attached to the lipid bilayer by their COOH-terminal ends, J. Mol. Biol. 124: 535–549.PubMedCrossRefGoogle Scholar
  5. Garoff, H., Frischauf, A.-M., Simons, K., Lehrach, H., and Delius, H., 1980a, Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins, Nature (London) 28: 236–241CrossRefGoogle Scholar
  6. Garoff, H., Frischauf, A.-M., Simons, K., Lehrach, H., and Delius, H., 1980b, The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region, Proc. Natl. Acad. Sci. U.S.A. 77: 6376–6380.PubMedCrossRefGoogle Scholar
  7. Harrison, S. C., 1983, Virus structure: High resolution perspectives, in: Advances in Virus Research, Vol. 28 ( M. Lauffer and K. Maromorosch, eds.), pp. 175–240, Academic Press, New York.Google Scholar
  8. Harrison, S. C., 1984a, Structure of viruses, in: The Microbe 1984, Part 1, Viruses (B. W. J. Mahy and J. R. Pattison, eds. ), pp. 29–73.Google Scholar
  9. Harrison, S. C., 1984b, Multiple modes of subunit association in the structures of simple spherical viruses, TIBS 9 (1): 345–351.Google Scholar
  10. Harrison, S. C., David, A., Jumblatt, J., and Darnell, J. E., 1971, Lipid and protein organization in Sindbis virus, J. Mol. Biol. 60: 532.CrossRefGoogle Scholar
  11. Helenius A., and Söderlund, H., 1973, Stepwise dissociation of the Semliki Forest virus membrane with Triton X-100, Biochim. Biophys. Acta 307: 287–300.PubMedCrossRefGoogle Scholar
  12. Helenius, A., Kartenbeck, J., Simons, K., and Fries, E., 1980, On the entry of Semliki Forest virus into BHK-21 cells, J. Cell Biol. 84: 404–420.PubMedCrossRefGoogle Scholar
  13. Hirschberg, C. B., and Robbins, P. W., 1974, The glycolipids and phospholipids of Sindbis virus and their relation to the lipids of the host-cell plasma membrane, Virology 61: 602–608.PubMedCrossRefGoogle Scholar
  14. Hopper, P., Harrison, S. C., and Sauer, R., 1984, Amino acid sequence of the coat protein of tomato bushy stunt virus: Chemical determination and structural implications, J. Mol. Biol. 177: 701–713.PubMedCrossRefGoogle Scholar
  15. Laine, R., Hettunen, M.-L., Gahmberg, C. G., Kaariainen, L., and Renkonen, O., 1972, J. Virol. 10: 433–438.PubMedGoogle Scholar
  16. Laine, R., Soderlung, H., and Renkonen, O., 1973, Chemical composition of Semliki forest virus, Intervirology 1: 110–118.PubMedCrossRefGoogle Scholar
  17. Luukkonen, A., Kaariainen, L., and Renkonen, O., 1976, Phospholipids of Semliki forest virus grown in cultured mosquito cells, Biochim. Biophys. Acta 450: 109–120.Google Scholar
  18. McCarthy, M., and Harrison, S. C., 1977, Glycosidase susceptibility: A probe for the distribution of glycoprotein oligosaccharides in Sindbis virus, J. Virol. 23: 61.PubMedGoogle Scholar
  19. Rand, R. P., and Luzzati, V., 1968, X-ray diffraction study in water of lipid extracted from human erythrocytes, Biophys. J. 8: 125–137.PubMedCrossRefGoogle Scholar
  20. Rice, C. M., and Strauss, J. H., 1981, Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins, Proc. Natl. Acad. Sci. U.S.A. 78: 2062–2066.PubMedCrossRefGoogle Scholar
  21. Rice, C. M., and Strauss, J. H., 1982, Association of Sindbis virus glycoproteins and their precursors, J. Mol. Biol. 154: 325–348.PubMedCrossRefGoogle Scholar
  22. Rice, E. M., Bell, J. R., Hunkapiller, M. W., Strauss, E. G., Strauss, J. H., 1982, Isolation and characterization of the hydrophobic COOH-terminal domains of Sindbis virion glycoproteins, J. Mol. Biol. 154: 355–378.PubMedCrossRefGoogle Scholar
  23. Simons, K., and Warren, G., 1984, Semliki Forest virus: A probe for membrane traffic in the animal cell, Adv. Protein Chem. 36: 79–132.PubMedCrossRefGoogle Scholar
  24. Skehel, J. J., Bayley, P. M., Brown, E. B., Martin, S. R., Waterfield, M. D., White, J. M. Wilson, I. A., and Wiley, D. C., 1982, Changes in the conformation of influenza virus haemagglutinin at the pH optimum of virus mediated membrane fusion, Proc. Natl. Acad. Sci. U.S.A. 79: 968.PubMedCrossRefGoogle Scholar
  25. Sorger, P. K., Stockley, P. G., and Harrison, S. C., 1986, Structure and assembly of turnip crinkle virus. II. Mechanisms of in vitro reassembly, J. Mol. Biol. (in press).Google Scholar
  26. Utermann, G., and Simons, K., 1974, Studies on the amphipathic nature of the membrane proteins in Semliki Forest virus, J. Mol. Biol. 85: 569–587.PubMedCrossRefGoogle Scholar
  27. Van Meer, G., Simons, K., Op den Kamp, J., and van Deenen, L. L. M., 1981, Phospholipid assymmetry in Semliki Forest virus grown on BHK-21 cells, Biochemistry 20: 1974–1981.PubMedCrossRefGoogle Scholar
  28. Varghese, J. N., Laver, W. G., and Coleman, P M., 1983, Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution, Nature (London) 303: 35–40.CrossRefGoogle Scholar
  29. Von Bonsdorff, C.-H., 1973, The structure of Semliki forest virus, Commentat. Biol. Soc. Sci. Fenn. 74: 1–53.Google Scholar
  30. Von Bonsdorff, C.-H., and Harrison, S. C., 1975, Sindbis virus glycoprotiens form a regular icosahedral surface lattice, J. Virol. 16: 141.Google Scholar
  31. Von Bonsdorff, C.-H., and Harrrison, S. C., 1978, Crystalline arrays of Sindbis virus glycoprotein, J. Virol. 28: 578.Google Scholar
  32. Wengler, G., Boege, U., Wengler, G., Bischoff, H., and Wahn, K., 1982, The core protein of the alphavirus Sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro, Virology 118: 401–410.PubMedCrossRefGoogle Scholar
  33. Wiley, D. C., and von Bonsdorff, C.-H., 1978, Three-dimensional crystals of the lipid enveloped Semliki Forest virus, J. Mol. Biol. 120: 375–379.PubMedCrossRefGoogle Scholar
  34. Wilson, I. A., Wiley, D. C., and Skehel, J. J., 1981, Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation, Nature (London) 289: 373–378.CrossRefGoogle Scholar
  35. Ziemiecki, A., and Garoff, H., 1978, Subunit composition of the membrane glycoprotein complex of Semliki Forest virus, J. Mol. Biol. 122: 259–269.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Stephen C. Harrison
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyHarvard UniversityCambridgeUSA

Personalised recommendations