Brasch, MelaniePutri, Rindia M.de Ruiter, Mark V.Luque, DanielKoay, Melissa S. T.Castón, José RCornelissen, Jeroen J. L. M.2019-05-302019-05-302017J. Am. Chem. Soc.2017,139,4,1512-15190002-7863http://hdl.handle.net/20.500.12105/7698The packaging of proteins into discrete compartments is an essential feature for cellular efficiency. Inspired by Nature, we harness virus-like assemblies as artificial nanocompartments for enzyme-catalyzed cascade reactions. Using the negative charges of nucleic acid tags, we develop a versatile strategy to promote an efficient noncovalent co-encapsulation of enzymes within a single protein cage of cowpea chlorotic mottle virus (CCMV) at neutral pH. The encapsulation results in stable 21-22 nm sized CCMV-like particles, which is characteristic of an icosahedral T = 1 symmetry. Cryo-EM reconstruction was used to demonstrate the structure of T = 1 assemblies templated by biological soft materials as well as the extra-swelling capacity of these T = 1 capsids. Furthermore, the specific sequence of the DNA tag is capable of operating as a secondary biocatalyst as well as bridging two enzymes for co-encapsulation in a single capsid while maintaining their enzymatic activity. Using CCMV-like particles to mimic nanocompartments can provide valuable insight on the role of biological compartments in enhancing metabolic efficiency.engVoRhttp://creativecommons.org/licenses/by-nc-nd/4.0/BiocatalysisBromovirusGlucose OxidaseNucleic AcidsParticle SizePhosphogluconate DehydrogenasePhosphotransferases (Alcohol Group Acceptor)Surface PropertiesAttribution-NonCommercial-NoDerivatives 4.0 Internacional280551881394151910.1021/jacs.6b109481520-5126Journal of the American Chemical Societyopen access