Self-assembling protein nanocages for modular enzyme assembly by orthogonal bioconjugation
Date
2021-06-25
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Biotechnology Progress
Abstract
The 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.
Description
This article was originally published in Biotechnology Progress. The version of record is available at: https://doi.org/10.1002/btpr.3190
Keywords
cellulosome, E2 nanocage, HBV, post translational ligation strategy, self-assembling protein nanocage, synthetic metabolon
Citation
Berckman, 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.3190