Designed Protein Cages

2013 ◽  
Author(s):  
D.S. Goodsell
Keyword(s):  
Protein Cages

Programmable in vitro Co-Encapsidation of Guest Proteins Inside Protein Nanocages

2018 ◽  
Author(s):  
Noor H. Dashti ◽  
Rufika S. Abidin ◽  
Frank Sainsbury
Keyword(s):  
Self Assembly ◽  
Mammalian Cells ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Super Resolution ◽  
Cell Engineering ◽  
Particle Analysis ◽  
Protein Cages

Bioinspired self-sorting and self-assembling systems using engineered versions of natural protein cages have been developed for biocatalysis and therapeutic delivery. The packaging and intracellular delivery of guest proteins is of particular interest for both <i>in vitro</i> and <i>in vivo</i> cell engineering. However, there is a lack of platforms in bionanotechnology that combine programmable guest protein encapsidation with efficient intracellular uptake. We report a minimal peptide anchor for <i>in vivo</i> self-sorting of cargo-linked capsomeres of the Murine polyomavirus (MPyV) major coat protein that enables controlled encapsidation of guest proteins by <i>in vitro</i> self-assembly. Using Förster resonance energy transfer (FRET) we demonstrate the flexibility in this system to support co-encapsidation of multiple proteins. Complementing these ensemble measurements with single particle analysis by super-resolution microscopy shows that the stochastic nature of co-encapsidation is an overriding principle. This has implications for the design and deployment of both native and engineered self-sorting encapsulation systems and for the assembly of infectious virions. Taking advantage of the encoded affinity for sialic acids ubiquitously displayed on the surface of mammalian cells, we demonstrate the ability of self-assembled MPyV virus-like particles to mediate efficient delivery of guest proteins to the cytosol of primary human cells. This platform for programmable co-encapsidation and efficient cytosolic delivery of complementary biomolecules therefore has enormous potential in cell engineering.

scholarly journals Introduction of Surface Loops as a Tool for Encapsulin Functionalization.

2021 ◽  
Author(s):  
Sandra Michel-Souzy ◽  
Naomi M. Hamelmann ◽  
Sara Zarzuela-Pura ◽  
Jos M. J. Paulusse ◽  
Jeroen J. L. M. Cornelissen
Keyword(s):  
Biomedical Applications ◽  
Large Scale ◽  
Thermotoga Maritima ◽  
Scale Production ◽  
Structure Property ◽  
Protein Subunit ◽  
Protein Cages ◽  
Notable Increase ◽  
The Stability ◽  
Surface Loops

Encapsulin based protein cages are nanoparticles with different biomedical applications, such as targeted drug delivery or imaging agents. These particles are biocompatible and can be produced in bacteria, allowing large scale production and protein engineering. In order to use these bacterial nanocages in different applications, it is important to further explore the potential of their surface modification and optimize their production. In this study we design and show new surface modifications of the Thermotoga maritima (Tm) and Brevibacterium linens (Bl) encapsulins. Two new loops on Tm encapsulin with a His-tag insertion after the residue 64 and the residue 127, and the modification of the C-terminal on Bl encapsulin, are reported. The multi-modification of the Tm encapsulin enables up to 240 different functionalities on the cage surface, resulting from 4 potential modifications per protein subunit. We furthermore report an improved protocol giving a better stability and providing a notable increase of the production yield of the cages. Finally, we tested the stability of different encapsulin variants over a year and the results show a difference in stability arising from the tag insertion position. These first insights in the structure-property relationship of encapsulins, with respect to the position of a function loop, allow for further study of the use of these protein nanocages in biomedical applications.

scholarly journals Laboratory evolution of virus-like nucleocapsids from nonviral protein cages

2018 ◽  
Vol 115 (21) ◽  
pp. 5432-5437 ◽  
Author(s):  
Naohiro Terasaka ◽  
Yusuke Azuma ◽  
Donald Hilvert
Keyword(s):  
Aquifex Aeolicus ◽  
Cellular Functions ◽  
Laboratory Evolution ◽  
Virion Assembly ◽  
Protein Cages ◽  
Protein Cage ◽  
Spherical Structures ◽  
Rna Genome ◽  
Biological Environment

Viruses are remarkable nanomachines that efficiently hijack cellular functions to replicate and self-assemble their components within a complex biological environment. As all steps of the viral life cycle depend on formation of a protective proteinaceous shell that packages the DNA or RNA genome, bottom-up construction of virus-like nucleocapsids from nonviral materials could provide valuable insights into virion assembly and evolution. Such constructs could also serve as safe alternatives to natural viruses for diverse nano- and biotechnological applications. Here we show that artificial virus-like nucleocapsids can be generated—rapidly and surprisingly easily—by engineering and laboratory evolution of a nonviral protein cage formed by Aquifex aeolicus lumazine synthase (AaLS) and its encoding mRNA. Cationic peptides were appended to the engineered capsid proteins to enable specific recognition of packaging signals on cognate mRNAs, and subsequent evolutionary optimization afforded nucleocapsids with expanded spherical structures that encapsulate their own full-length RNA genome in vivo and protect the cargo molecules from nucleases. These findings provide strong experimental support for the hypothesis that subcellular protein-bounded compartments may have facilitated the emergence of ancient viruses.

Synthesis of Nanoscale Iron Oxide Structures Using Protein Cages and Polysaccharide Networks

1994 ◽  
pp. 49-56 ◽  
Author(s):  
T. G. St. Pierre ◽  
P. Sipos ◽  
P. Chan ◽  
W. Chua-Anusorn ◽  
K. R. Bauchspiess ◽  
...  
Keyword(s):  
Iron Oxide ◽  
Protein Cages

Hydrophobic Cargo Encapsulation into Virus Protein Cages by Self-Assembly in an Aprotic Organic Solvent

2021 ◽  
Author(s):  
Amberly Xie ◽  
Irina Tsvetkova ◽  
Yang Liu ◽  
Xingchen Ye ◽  
Priyadarshine Hewavitharanage ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Self Assembly ◽  
Virus Protein ◽  
Protein Cages

Designed Protein Cages as Scaffolds for Building Multienzyme Materials

2020 ◽  
Vol 9 (2) ◽  
pp. 381-391 ◽  
Author(s):  
Scott A. McConnell ◽  
Kevin A. Cannon ◽  
Christian Morgan ◽  
Rachel McAllister ◽  
Brendan R. Amer ◽  
...  
Keyword(s):  
Protein Cages

DE NOVODesign of Protein Cages to Accommodate Metal Cofactors

2013 ◽  
pp. 43-85 ◽  
Author(s):  
Flavia Nastri ◽  
Rosa Bruni ◽  
Ornella Maglio ◽  
Angela Lombardi
Keyword(s):  
Protein Cages ◽  
Metal Cofactors

scholarly journals Nanoscale assemblies and their biomedical applications

2013 ◽  
Vol 10 (80) ◽  
pp. 20120740 ◽  
Author(s):  
Tais A. P. F. Doll ◽  
Senthilkumar Raman ◽  
Raja Dey ◽  
Peter Burkhard
Keyword(s):  
Biomedical Applications ◽  
Vaccine Development ◽  
Building Blocks ◽  
Eukaryotic Cells ◽  
Peptide Nanotubes ◽  
Protein Cages ◽  
Bacterial Microcompartments ◽  
Self Assembling ◽  
Development Section ◽  
Characteristic Features

Nanoscale assemblies are a unique class of materials, which can be synthesized from inorganic, polymeric or biological building blocks. The multitude of applications of this class of materials ranges from solar and electrical to uses in food, cosmetics and medicine. In this review, we initially highlight characteristic features of polymeric nanoscale assemblies as well as those built from biological units (lipids, nucleic acids and proteins). We give special consideration to protein nanoassemblies found in nature such as ferritin protein cages, bacterial microcompartments and vaults found in eukaryotic cells and designed protein nanoassemblies, such as peptide nanofibres and peptide nanotubes. Next, we focus on biomedical applications of these nanoscale assemblies, such as cell targeting, drug delivery, bioimaging and vaccine development. In the vaccine development section, we report in more detail the use of virus-like particles and self-assembling polypeptide nanoparticles as new vaccine delivery platforms.

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