SpyRings Declassified

Schoene, Christopher; Bennett, Samantha; Howarth, Mark

doi:10.1016/bs.mie.2016.05.004

Cited by 27 publications

(14 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4A). 63 Similar effects on resilience were found for SpyRing versions of phytase, 64 xylanase 65 and luciferase. 66 Apart from temperature, increased tolerance to organic solvents and denaturant has been found upon SpyRing cyclisation.…”

Section: Enzyme Resilience and Assemblysupporting

confidence: 53%

Power to the protein: enhancing and combining activities using the Spy toolbox

2020

View full text Add to dashboard Cite

show abstract

Section: Enzyme Resilience and Assemblysupporting

confidence: 53%

Power to the protein: enhancing and combining activities using the Spy toolbox

2020

View full text Add to dashboard Cite

show abstract

“… 66 However, SpyCatcher has shown the ability to enhance protein thermal resilience in the context of cyclizing enzymes. 67 , 68 …”

Section: Discussionmentioning

confidence: 99%

Engineering a Rugged Nanoscaffold To Enhance Plug-and-Display Vaccination

et al. 2018

View full text Add to dashboard Cite

Nanoscale organization is crucial to stimulating an immune response. Using self-assembling proteins as multimerization platforms provides a safe and immunogenic system to vaccinate against otherwise weakly immunogenic antigens. Such multimerization platforms are generally based on icosahedral viruses and have led to vaccines given to millions of people. It is unclear whether synthetic protein nanoassemblies would show similar potency. Here we take the computationally designed porous dodecahedral i301 60-mer and rationally engineer this particle, giving a mutated i301 (mi3) with improved particle uniformity and stability. To simplify the conjugation of this nanoparticle, we employ a SpyCatcher fusion of mi3, such that an antigen of interest linked to the SpyTag peptide can spontaneously couple through isopeptide bond formation (Plug-and-Display). SpyCatcher-mi3 expressed solubly to high yields in Escherichia coli, giving more than 10-fold greater yield than a comparable phage-derived icosahedral nanoparticle, SpyCatcher-AP205. SpyCatcher-mi3 nanoparticles showed high stability to temperature, freeze–thaw, lyophilization, and storage over time. We demonstrate approximately 95% efficiency coupling to different transmission-blocking and blood-stage malaria antigens. Plasmodium falciparum CyRPA was conjugated to SpyCatcher-mi3 nanoparticles and elicited a high avidity antibody response, comparable to phage-derived virus-like particles despite their higher valency and RNA cargo. The simple production, precise derivatization, and exceptional ruggedness of this nanoscaffold should facilitate broad application for nanobiotechnology and vaccine development.

show abstract

“…These form peptide bonds with N-terminal thiol groups via trans-thioesterification and acyl transfer reactions, [85] engineered disulfide bonds, [86] and isopeptide bonds, especially cyclization mediated by SpyTag/SpyCatcher strategies. [87]…”

Section: Peptide and Protein Cyclizationmentioning

confidence: 99%

Intramolecular Covalent Bonds in Gram‐Positive Bacterial Surface Proteins

Lei

Cao

2022

ChemBioChem

View full text Add to dashboard Cite

Gram-positive bacteria experience considerable mechanical perturbation when adhering to host surfaces during colonization and infection. They have evolved various adhesion proteins that are mechanically robust to ensure strong surface adhesion. Recently, it was discovered that these adhesion proteins contain rare, extra intramolecular covalent bonds that stabilize protein structures and participate in surface bonding. These intramolecular covalent bonds include isopeptides, thioesters, and ester bonds, which often form spontaneously without the need for additional enzymes. With the development of singlemolecule force spectroscopy techniques, the detailed mechanical roles of these intramolecular covalent bonds have been revealed. In this review, we summarize the recent advances in this area of research, focusing on the link between the mechanical stability and function of these covalent bonds in Gram-positive bacterial surface proteins. We also highlight the potential impact of these discoveries on the development of novel antibiotics and chemical biology tools.

show abstract

SpyRings Declassified

Cited by 27 publications

References 52 publications

Power to the protein: enhancing and combining activities using the Spy toolbox

Power to the protein: enhancing and combining activities using the Spy toolbox

Engineering a Rugged Nanoscaffold To Enhance Plug-and-Display Vaccination

Intramolecular Covalent Bonds in Gram‐Positive Bacterial Surface Proteins

Contact Info

Product

Resources

About