Allosteric Control of Icosahedral Capsid Assembly.

J Phys Chem B

Martin Fisher School of Physics, Brandeis University, Waltham, Massachusetts 02454, United States.

Published: July 2016

AI Article Synopsis

  • During a virus's life cycle, its proteins assemble into a protective shell called a capsid, balancing stability and the avoidance of assembly issues.
  • The study explores how this assembly process is influenced by allosteric regulation, where capsid proteins switch between different shapes to optimize assembly.
  • Findings indicate that strong allosteric control enables effective assembly over a variety of conditions, highlighting its importance in models for estimating protein interactions.

Article Abstract

During the life cycle of a virus, viral proteins and other components self-assemble to form an ordered protein shell called a capsid. This assembly process is subject to multiple competing constraints, including the need to form a thermostable shell while avoiding kinetic traps. It has been proposed that viral assembly satisfies these constraints through allosteric regulation, including the interconversion of capsid proteins among conformations with different propensities for assembly. In this article, we use computational and theoretical modeling to explore how such allostery affects the assembly of icosahedral shells. We simulate assembly under a wide range of protein concentrations, protein binding affinities, and two different mechanisms of allosteric control. We find that above a threshold strength of allosteric control, assembly becomes robust over a broad range of subunit binding affinities and concentrations, allowing the formation of highly thermostable capsids. Our results suggest that allostery can significantly shift the range of protein binding affinities that lead to successful assembly and thus should be taken into account in models that are used to estimate interaction parameters from experimental data.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5367391PMC
http://dx.doi.org/10.1021/acs.jpcb.6b02768DOI Listing

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