DOI: 10.1101/511352Jan 3, 2019Paper

Selection and characterization of a reovirus mutant with improved thermostability

BioRxiv : the Preprint Server for Biology
Anthony J Snyder, Pranav Danthi


The environment represents a significant barrier to infection. Physical stressors (heat) or chemical agents (ethanol and sodium dodecyl sulfate) can render virions noninfectious. As such, discrete proteins are necessary to stabilize the dual layered structure of mammalian orthoreovirus (reovirus). The outer capsid participates in cell entry: (i) σ3 is degraded to generate the infectious subviral particle and (ii) μ1 facilitates membrane penetration and subsequent core delivery. μ1-σ3 interactions also prevent inactivation; however, this activity is not fully characterized. Using forward and reverse genetic approaches, we identified two mutations (μ1 M258I and σ3 S344P) within heat resistant strains. σ3 S344P was sufficient to enhance capsid integrity and to reduce protease sensitivity. Moreover, these changes impaired replicative fitness in a reassortant background. This work reveals new details regarding the determinants of reovirus stability.

Related Concepts

Peptide Hydrolases
Reoviridae Infections
Sodium Dodecyl Sulfate
Virus Assembly

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