Three-Dimensional Structure of Poliovirus at 2.9 angstrom Resolution

The three-dimensional structure of poliovirus has been determined at 2.9 angstrom resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a ``core'' consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the ``connecting loops'' and NH₂- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit ``cores'' to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH<sub>2</sub>- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the ``connecting loops'' and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.