Assembling Enzymatic Cascade Pathways inside Virus-Based Nanocages Using Dual-Tasking Nucleic Acid Tags

Melanie Brasch, Rindia M. Putri, Mark V. de Ruiter, Daniel Luque, Melissa S.T. Koay, José R. Castón, Jeroen J.L.M. Cornelissen

Research output: Contribution to journalArticleAcademicpeer-review

49 Citations (Scopus)
49 Downloads (Pure)

Abstract

The 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.
Original languageEnglish
Pages (from-to)1512-1519
JournalJournal of the American Chemical Society
Volume139
Issue number4
DOIs
Publication statusPublished - 1 Feb 2017

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