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  • The EMBO Journal (2003) 22, 2886 - 2892
  • doi:10.1093/emboj/cdg276

Three-dimensional structure of the M-MuLV CA protein on a lipid monolayer: a general model for retroviral capsid assembly

Barbie K. Ganser1, Anchi Cheng2, Wesley I. Sundquist1 and Mark Yeager2,3

  1. Department of Biochemistry, University of Utah, 20 North 1900 East, Salt Lake City, UT 84132, USA
  2. Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 USA
  3. Division of Cardiovascular Diseases, Scripps Clinic, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA

Correspondence to:

Mark Yeager, E-mail: Yeager@scripps.edu

Wesley I. Sundquist, E-mail: Wes@biochem.Utah.edu

Received 19 December 2002; Accepted 16 April 2003; Revised 27 February 2003

Although retroviruses from different genera form morphologically distinct capsids, we have proposed that all of these structures are composed of similar hexameric arrays of capsid (CA) protein subunits and that their distinct morphologies reflect different distributions of pentameric declinations that allow the structures to close. Consistent with this model, CA proteins from both HIV-1 and Rous sarcoma virus (RSV) form similar hexagonal lattices. However, recent structural studies have suggested that the Moloney murine leukemia virus (M-MuLV) CA protein may assemble differently. We now report an independent three-dimensional reconstruction of two-dimensional crystals of M-MuLV CA. This new reconstruction reveals a hexameric lattice that is similar to those formed by HIV-1 and RSV CA, supporting a generalized model for retroviral capsid assembly.

  • Keywords:

    • CA,
    • electron crystallography,
    • Moloney murine leukemia virus (M-MuLV),
    • retroviral capsid assembly