Adenovirus core protein V reinforces the capsid and enhances genome release from disrupted particles

Author:

Martín-González Natalia1ORCID,Gómez-González Alfonso2ORCID,Hernando-Pérez Mercedes3ORCID,Bauer Michael2ORCID,Greber Urs F.2ORCID,San Martín Carmen3ORCID,de Pablo Pedro J.1ORCID

Affiliation:

1. Departament of Condensed Matter Physics, Universidad Autónoma de Madrid and Institute of Condensed Matter Physics (IFIMAC), 28049 Madrid, Spain.

2. Department of Molecular Life Sciences, University of Zurich, CH-8057 Zurich, Switzerland.

3. Department of Macromolecular Structures, Centro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.

Abstract

Out of the three core proteins in human adenovirus, protein V is believed to connect the inner capsid surface to the outer genome layer. Here, we explored mechanical properties and in vitro disassembly of particles lacking protein V (Ad5-ΔV). Ad5-ΔV particles were softer and less brittle than the wild-type ones (Ad5-wt), but they were more prone to release pentons under mechanical fatigue. In Ad5-ΔV, core components did not readily diffuse out of partially disrupted capsids, and the core appeared more condensed than in Ad5-wt. These observations suggest that instead of condensing the genome, protein V antagonizes the condensing action of the other core proteins. Protein V provides mechanical reinforcement and facilitates genome release by keeping DNA connected to capsid fragments that detach during disruption. This scenario is in line with the location of protein V in the virion and its role in Ad5 cell entry.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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