Skip to main content
Springer Nature - PMC COVID-19 Collection logoLink to Springer Nature - PMC COVID-19 Collection
. 2006;581:181–185. doi: 10.1007/978-0-387-33012-9_31

Ultrastructure of SARS-CoV, FIPV, and MHV Revealed by Electron Cryomicroscopy

Benjamin W Neuman 3, Brian D Adair 4, Craig Yoshioka 5, Joel D Quispe 6, Ronald A Milligan 7, Mark Yeager 8, Michael J Buchmeier 9
Editors: Stanley Perlman1, Kathryn V Holmes2
PMCID: PMC7123189  PMID: 17037527

The content is available as a PDF (1.3 MB).

Contributor Information

Stanley Perlman, Email: Stanley-Perlman@uiowa.edu

Kathryn V. Holmes, Email: Kathryn.Holmes@ucHSC.edu

References

  • 1.Risco C, Anton IM, Enjuanes L, Carrascosa JL. The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins. J. Virol. 1996;70:4773–4777. doi: 10.1128/jvi.70.7.4773-4777.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 2.Booy FP, Ruigrok RW, van Bruggen EF. Electron microscopy of influenza virus. A comparison of negatively stained and ice-embedded particles, J. Mol. Biol. 1985;184:667–676. doi: 10.1016/0022-2836(85)90312-2. [DOI] [PubMed] [Google Scholar]
  • 3.Fujiyoshi Y, Kume NP, Sakata K, Sato SB. Fine structure of influenza A virus observed by electron cryo-microscopy. EMBO J. 1994;13:318–326. doi: 10.1002/j.1460-2075.1994.tb06264.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 4.Shangguan T, Siegel DP, Lear JD, Axelsen PH, Alford D, Bentz J. Morphological changes and fusogenic activity of influenza virus hemagglutinin. Biophys. J. 1998;74:54–62. doi: 10.1016/S0006-3495(98)77766-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 5.Wilk T, Geiselhart V, Frech M, Fuller SD, Flugel RM, Lochelt M. Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain. J. Virol. 2001;75:7995–8007. doi: 10.1128/JVI.75.17.7995-8007.2001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 6.Briggs JA, Wilk T, Welker R, Krausslich HG, Fuller SD. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 2003;22:1707–1715. doi: 10.1093/emboj/cdg143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 7.Fuller SD, Wilk T, Gowen BE, Krausslich HG, Vogt VM. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 1997;7:729–738. doi: 10.1016/S0960-9822(06)00331-9. [DOI] [PubMed] [Google Scholar]
  • 8.Goto T, Ashina T, Fujiyoshi Y, Kume N, Yamagishi H, Nakai M. Projection structures of human immunodeficiency virus type1(HIV-1) observed with high resolution electron cryo-microscopy. J. Electron Microsc. (Tokyo) 1994;43:16–19. [PubMed] [Google Scholar]
  • 9.Nermut MV, Grief C, Hashmi S, Hockley DJ. Further evidence of icosahedral symmetry in human and simian immunodeficiency virus, AIDS Res. Hum. Retroviruses. 1993;9:929–938. doi: 10.1089/aid.1993.9.929. [DOI] [PubMed] [Google Scholar]
  • 10.Wilk T, Gross I, Gowen BE, Rutten T, de Haas F, Welker R, Krausslich HG, Boulanger P, Fuller SD. Organization of immature human immunodeficiency virus type 1. J. Virol. 2001;75:759–771. doi: 10.1128/JVI.75.2.759-771.2001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 11.Yeager M, Wilson-Kubalek EM, Weiner SG, Brown PO, Rein A. Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl. Acad. Sci. USA. 1998;95:7299–7304. doi: 10.1073/pnas.95.13.7299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 12.Kingston RL, Olson NH, Vogt VM. The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy. J. Struct. Biol. 2001;136:67–80. doi: 10.1006/jsbi.2001.4423. [DOI] [PubMed] [Google Scholar]
  • 13.Yu F, Joshi SM, Ma YM, Kingston RL, Simon MN, Vogt VM. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J. Virol. 2001;75:2753–2764. doi: 10.1128/JVI.75.6.2753-2764.2001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 14.Talmon Y, Prasad BV, Clerx JP, Wang GJ, Chiu W, Hewlett MJ. Electron microscopy of vitrified-hydrated La Crosse virus. J. Virol. 1987;61:2319–2321. doi: 10.1128/jvi.61.7.2319-2321.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 15.Wang GJ, Hewlett M, Chiu W. Structural variation of La Crosse virions under different chemical and physical conditions. Virology. 1991;184:455–459. doi: 10.1016/0042-6822(91)90869-D. [DOI] [PubMed] [Google Scholar]
  • 16.Hosaka Y, Watabe T. Cryoelectron microscopy of vitrified Sendai virions. J. Virol. Methods. 1988;22:347–349. doi: 10.1016/0166-0934(88)90117-6. [DOI] [PubMed] [Google Scholar]
  • 17.Neuman BW, Adair BD, Burns JW, Milligan RA, Buchmeier MJ, Yeager M. Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis. J. Virol. 2005;79:3822–3830. doi: 10.1128/JVI.79.6.3822-3830.2005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 18.Macnaughton MR, Davies HA, Nermut MV. Ribonucleoprotein-like structures from coronavirus particles. J. Gen. Virol. 1978;39:545–549. doi: 10.1099/0022-1317-39-3-545. [DOI] [PubMed] [Google Scholar]
  • 19.Escors D, Ortego J, Laude H, Enjuanes L. The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability. J. Virol. 2001;75:1312–1324. doi: 10.1128/JVI.75.3.1312-1324.2001. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Nidoviruses are provided here courtesy of Nature Publishing Group

RESOURCES