Alternative Assembly of Qβ Virus Like Particles

Abstract

AbstractQβ virus like particles (VLPs) are versatile platforms for grafting functional groups for vaccine development. The structure of Qβ VLPs at atomic detail are critical for design of more effective vaccines. While the structures of native Qβ VLPs have been determined previously, the structure of VLPs assembled from a recombinantly expressed Qβ coat protein, which are extensively used as platforms have not been studied. We sought to determine the crystal structures of VLPs assembled from recombinantly expressed Qβ coat protein of wild type and two mutants: A38K and A38K/A40C/D102C. The structures of Qβ VLPs assembled from recombinantly expressed Qβ coat proteins showed that VLPs can be assembled both in T=1 and T=3 symmetry.