Alternative Assembly of Qβ Virus Like Particles

Abstract

Q{beta} virus like particles (VLPs) are versatile platforms for grafting functional groups for vaccine development. The structure of Q{beta} VLPs at atomic detail are critical for design of more effective vaccines. While the structures of native Q{beta} VLPs have been determined previously, the structure of VLPs assembled from a recombinantly expressed Q{beta} 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 Q{beta} coat protein of wild type and two mutants: A38K and A38K/A40C/D102C. The structures of Q{beta} VLPs assembled from recombinantly expressed Q{beta} coat proteins showed that VLPs can be assembled both in T=1 and T=3 symmetry.