The structure and flexibility of conical HIV-1 capsids determined within intact virions

• DOI: 10.1126/science.aah4972
• Publication Date: 2016-12-15T19:00:47Z
• Authors: Simone Mattei; Bärbel Glass; Wim J. H. Hagen; Hans-Georg Kräuss...; John A. G. Briggs
• Keywords: Pentamer; Random hexamer

HIV-1 contains a cone-shaped capsid encasing the viral genome. This is thought to follow fullerene geometry-a curved hexameric lattice of protein, CA, closed by incorporating 12 CA pentamers. Current models for core structure are based on crystallography and cross-linked pentameric electron microscopy tubular arrays, simulations. Here, we report subnanometer-resolution cryo-electron tomography structures within intact particles. Whereas hexamer compatible with studies, pentamer forms using different interfaces. Determining multiple revealed how flexes form variably shell. We show that assembles both aberrant perfect cones, supporting in which conical cores assemble de novo after maturation.