Why are viral capsids icosahedral?

COLL 5

William M. Gelbart1, Robijn Bruinsma2, David Reguera3, Joseph Rudnick4, and Roya Zandi1. (1) Department of Chemistry and Biochemistry, University of California Los Angeles, 405 Hilgard Avenue, Los Angeles, CA 90095, (2) Department of Physics and Astronomy, University of California, Los Angeles, Hilgard Av, Los Angeles, CA 90095, (3) Department of Chemistry and Biochemistry, University of California, Los Angeles, 405 Hilgard Avenue, Los Angeles, CA 90095, (4) Dept. of Physics and Astronomy, University of California, Los Angeles, CA 90095
All viruses involve the confinement of their genome in a rigid protein shell (the "capsid"). In almost all cases this capsid is either cylindrical or "spherical"/isometric, and in virtually all of the latter cases it has icosahedral symmetry (6 five-fold axes of rotation, 10 three-fold, and 15 two-fold). Furthermore, in an overwhelming majority of instances, the viral capsid is formed via a spontaneous self-assembly process involving special numbers of proteins that are particular integral multiples of 60. In this talk I present a generic Hamiltonian for the interaction between (small multimers of) constituent proteins whose minimization leads to icosahedral symmetry for these magic numbers. This same Hamiltonian allows for direct calculation of the stress distribution throughout the capsid and to a natural description of its expansion and rupture properties relevant to genome release.
 

Bio-Colloids
8:30 AM-11:30 AM, Sunday, March 28, 2004 Marriott -- Grand Ballroom J, Oral

Division of Colloid and Surface Chemistry

The 227th ACS National Meeting, Anaheim, CA, March 28-April 1, 2004