Self-assembling protein nanocages for modular enzyme assembly by orthogonal bioconjugation

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Author(s)Berckman, Emily A.
Author(s)Chen, Wilfred
Date Accessioned2022-01-12T21:38:43Z
Date Available2022-01-12T21:38:43Z
Publication Date2021-06-25
DescriptionThis article was originally published in Biotechnology Progress. The version of record is available at: https://doi.org/10.1002/btpr.3190en_US
AbstractThe wide variety of enzymatic pathways that can benefit from enzyme scaffolding is astronomical. While enzyme co-localization based on protein, DNA, and RNA scaffolds has been reported, we still lack scaffolds that offer well-defined and uniform three-dimensional structures for enzyme organization. Here we reported a new approach for protein co-localization using naturally occurring protein nanocages as a scaffold. Two different nanocages, the 25 nm E2 and the 34 nm heptatitis B virus, were used to demonstrate the successfully co-localization of the endoglucanase CelA and cellulose binding domain using the robust SpyTag/SpyCatcher bioconjugation chemistry. Because of the simplicity of the assembly, this strategy is useful not only for in vivo enzyme cascading but also the potential for in vivo applications as well.en_US
SponsorNational Science Foundation, Grant/Award Numbers: DMR1609621, MCB1615731en_US
CitationBerckman, EA, Chen, W. Self-assembling protein nanocages for modular enzyme assembly by orthogonal bioconjugation. Biotechnol Progress. 2021; 37( 5):e3190. https://doi.org/10.1002/btpr.3190en_US
ISSN1520-6033
URLhttps://udspace.udel.edu/handle/19716/29970
Languageen_USen_US
PublisherBiotechnology Progressen_US
Keywordscellulosomeen_US
KeywordsE2 nanocageen_US
KeywordsHBVen_US
Keywordspost translational ligation strategyen_US
Keywordsself-assembling protein nanocageen_US
Keywordssynthetic metabolonen_US
TitleSelf-assembling protein nanocages for modular enzyme assembly by orthogonal bioconjugationen_US
TypeArticleen_US
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