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Updated: Dec 12, 2025

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
Enzyme Stabilization by Virus-Like Particles
Soumen Das1, Liangjun Zhao1, Kristen Elofson1
1School of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, Georgia 30306, United States.
Abstract:
The properties of enzymes packaged within the coat protein shell of virus-like particles (VLPs) were studied to provide a comprehensive assessment of such factors. Such entrainment did not seem to perturb enzyme function, but it did significantly enhance enzyme stability against several denaturing stimuli such as heat, organic solvents, and chaotropic agents. This improvement in performance was found to be general and independent of the number of independent subunits required and of the number of catalytically active enzymes packaged. Packaged enzymes were found by measurements of intrinsic tryptophan fluorescence to retain some of their native folded structure even longer than their catalytic activity, suggesting that protein folding is a significant component of the observed catalytic benefits. While we are unable to distinguish between kinetic and thermodynamic effects - including inhibition of enzyme unfolding, acceleration of refolding, and biasing of folding equilibria - VLP packaging appears to represent a useful general strategy for the stabilization of enzymes that operate on diffusible substrates and products.
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