Thermostable exoshells fold and stabilize recombinant proteins

Deshpande, Siddharth; Masurkar, Nihar; Girish, Vallerinteavide Mavelli; Desai, Malan Manish; Chakraborty, Goutam; Chan, Juliana M.; Drum, Chester L.

doi:10.1038/s41467-017-01585-2

Cited by 26 publications

(55 citation statements)

References 35 publications

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“…S10). These results are similar to those presented by Deshpande et al, where an engineered AfFtn with different overall interior cage charges was best able to stabilize the folding of guest proteins that had charge complementarity between host and guest …”

Section: Resultssupporting

confidence: 90%

A protein–protein host–guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein

et al. 2018

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We characterize the encapsulation of supercharged green fluorescent protein, GFP(+36), by thermophilic ferritin from Archaeoglobus fulgidus (AfFtn). The AfFtn-GFP(+36) assembly is rapid, nearly stoichiometric, and robust. Using a more stably assembled mutant AfFtn, we show that encapsulation can occur in the presence of mostly assembled cages, in addition to encapsulation starting from AfFtn individual subunits. Assembly and encapsulation do not occur with non-supercharged GFP or the alternately supercharged GFP(-30), highlighting the role of complementary electrostatic interactions between the cargo and AfFtn cage interior. We also present a method for verifying protein-protein encapsulation, using nickel nitrilotriacetic acid agarose resin. AfFtn-supercharged protein host-guest complexes could find applications in enzyme studies, protein separations, and in vivo protein stabilization and targeted delivery.

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Section: Resultssupporting

confidence: 90%

A protein–protein host–guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein

et al. 2018

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“…In addition, the encapsulated cargo appears resistant to thermal, chaotropic, and proteolytic stress and in some cases appeared to result in several-fold increase in protein folding efficiency. 81…”

Section: Ferritinmentioning

confidence: 99%

Enzyme encapsulation by protein cages

et al. 2020

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“…Ferritin from Archaeoglobus fulgidus with the F166H mutation was prepared as described. 18 NapA from Thermus thermophilus was expressed in E. coli and purified as described. 19 NHA2 from Bison bison (residues 69-525) was expressed in yeast and purified using the protocol described previously for human NHA2.…”

Section: Protein Preparationmentioning

confidence: 99%

Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches

et al. 2020

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In structural biology, collision cross sections (CCS) from ion mobility mass spectrometry (IM-MS) measurements are routinely compared to computationally or experimentally derived protein structures. Here, we investigate whether CCS data can inform about the shape of a protein in the absence of specific reference structures. Analysis of the proteins in the CCS database shows that protein complexes with low apparent densities are structurally more diverse than those with a high apparent density. Using the CCS, molecular weight, and oligomeric states to mine the Protein Data Bank (PDB) for potentially similar protein structures, we find that we can distinguish oblate-and prolate-shaped protein complexes. We then apply the strategy to an integral membrane protein by comparing the shapes of a prokaryotic and an eukaryotic sodium/proton antiporter homologue. We conclude that mining the PDB with IM-MS data is a time-effective way to derive low-resolution structural models. File list (2) download file view on ChemRxiv main_chemrxiv.docx (2.05 MiB) download file view on ChemRxiv Supplementary Tables 1-4.pdf (50.74 KiB)

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Thermostable exoshells fold and stabilize recombinant proteins

Cited by 26 publications

References 35 publications

A protein–protein host–guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein

A protein–protein host–guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein

Enzyme encapsulation by protein cages

Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches

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