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4 results on '"Plug-and-display"'

1. The position of Spy Tag/Catcher system in hepatitis B core protein particles affects the immunogenicity and stability of the synthetic vaccine.

Author

Sheng, Yanan, Li, Zhengjun, Lin, Xuan, Ma, Yanyan, Ren, Ying, Su, Zhiguo, Ma, Guanghui, and Zhang, Songping

Subjects
*IMMUNE response, *EXTRACELLULAR matrix proteins, *VIRUS-like particles, *PEPTIDES, *HEPATITIS B, *CATCHERS (Baseball)
Abstract

Presenting exogenous antigens on virus-like particles (VLPs) through "plug-and-display" decoration strategies based on SpyTag/SpyCatcher isopeptide bonding have emerged as attractive technology for vaccine synthesis. However, whether the position of ligation site in VLPs will impose effects on immunogenicity and physiochemical properties of the synthetic vaccine remains rarely investigated. Here in the present work, the well-established hepatitis B core (HBc) protein was used as chassis to construct dual-antigen influenza nanovaccines, with the conserved epitope peptides derived from extracellular domain of matrix protein M2 (M2e) and hemagglutinin (HA) as target antigens. The M2e antigen was genetically fused to the HBc in the MIR region, together with the SpyTag peptide, which was fused either in the MIR region or at the N-terminal of the protein, so that a recombinant HA antigen (rHA) linked to SpyCatcher can be displayed on it, at two different localizations. Both synthetic nanovaccines showed ability in inducing strong M2e and rHA-specific antibodies and cellular immunogenicity; nevertheless, the one in which rHA was conjugated by N-terminal Tag ligation, was superior to another one synthesized by linking the rHA to MIR region SpyTagged-HBc in all aspects, including higher antigen-specific immunogenicity responses, lower anti-HBc carrier antibody, as well as better dispersion stability. Surface charge and hydrophobicity properties of the two synthetic nanovaccines were analyzed, results revealed that linking the rHA to MIR region SpyTagged-HBc lead to more significant and disadvantageous alteration in physiochemical properties of the HBc chassis. This study will expand our knowledge on "plug-and-display" decoration strategies and provide helpful guidance for the rational design of HBc-VLPs based modular vaccines by using SpyTag/Catcher synthesis. [ABSTRACT FROM AUTHOR]

Published
2023
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2. Engineering modular platforms for rapid vaccine development

Author

Brune, Karl Dietrich and Howarth, Mark

Subjects
572, Protein Engineering, Biochemistry, Synthetic biology, Vaccines, VLP, Vaccine, Isopeptide bond, Virus-like particle, Particulate vaccine, TBV, Dually-addressable nanoparticle, VLPs, Malaria, SpyCatcher, Cancer Immunotherapy, Plug-and-display, SnoopCatcher, Transmission-blocking vaccine
Abstract

Vaccines have saved more lives than any other medical intervention. Recombinant vaccines provide unmatched safety profiles, but at the expense of reduced immunogenicity. Virus-like particles (VLPs) resemble viruses in size, shape and repetitive arrangement but are devoid of pathogenic genetic material and therefore safe. Poor immunogens can be rendered immunogenic by display on VLPs. Successfully decorating VLPs is still a major challenge. Genetic fusion or chemical modification is often time-consuming and can lead to misassembly or misfolding, which obstructs generation of the desired immune response. SpyCatcher is a genetically encodable protein, previously engineered to form a covalent isopeptide bond to its peptide-partner SpyTag. Presented in this thesis are SpyCatcher-VLPs, based on the fusion of SpyCatcher to the bacteriophage VLP AP205. SpyCatcher- VLPs can be conveniently conjugated with SpyTag fused antigens, simply by mixing. I demonstrate the modularity of this approach by covalently linking several complex, cysteine-rich malarial antigens to SpyCatcher-VLPs, such as the transmission-blocking antigen Pfs25 and the blood-stage antigen CIDR. A single administration of Pfs25-SpyTag conjugated to SpyCatcher-VLPs induced potent antibody generation against Pfs25, even in the absence of adjuvant. Anti-Pfs25 antibodies induced by this platform conveyed potent transmission-blocking activity in the mosquito vector. The thesis further demonstrates the feasibility of more complex Catcher-nanoparticle architectures. The previously engineered SnoopCatcher covalently reacts with SnoopTag peptide and is orthogonal to the SpyCatcher / SpyTag pair. IMX313 is an engineered chimera of the multimerization domain of chicken complement inhibitor C4-binding protein. This work describes fusion of SnoopCatcher and SpyCatcher to IMX313, which yields independently addressable Catcher-moieties on a single IMX313 nanoparticle. Display of two antigens on one particle may enable single-particle, multi-disease vaccines as well as multi-stage vaccines to tackle immune evasion of parasites. The platforms presented should accelerate and enhance vaccine development and may create opportunities for imaging and metabolic engineering.

Published
2016

3. 2020 25th IEEE International Conference on Emerging Technologies and Factory Automation (ETFA), Vienna / Towards a Modular Architecture for Industrial HMIs

Author

Shakil, Muddasir and Zoitl, Alois

Subjects
Plug-and-Play, modular production systems, micro-frontend architecture, Cyber-Physical System, Plug-and-Display, Hardware_CONTROLSTRUCTURESANDMICROPROGRAMMING, micro-services, flexible manufacturing systems, HMI
Abstract

This paper presents a work in progress on a modular architecture design of industrial HMIs. The proposed approach is based on a micro frontend architecture style for developing web applications. It allows developers and integration engineers to build an HMI from distributed and modular shop-floor components called micro frontend. Each micro frontend is end-to-end integrated from its data acquisition to the user interfaces. This approach introduces an agile and modular development style of an industrial HMI for a modular and adaptive production system. (VLID)5693629 Accepted version

Published
2020
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4. Insider information on successful covalent protein coupling with help from SpyBank.

Author

Keeble AH and Howarth M

Subjects
Blotting, Western methods, Databases, Protein, Electrophoresis, Polyacrylamide Gel methods, Escherichia coli genetics, Gene Expression, HEK293 Cells, Humans, Peptides chemistry, Protein Engineering methods, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Peptides genetics
Abstract

New biological properties can stem from the freedom to link, multimerize, or multiplex protein building blocks. The peptide SpyTag on one protein irreversibly reacts with SpyCatcher on another protein, through spontaneous isopeptide bond formation. Reaction is specific in a wide range of cellular environments and all components are genetically encoded, making this chemistry accessible to molecular biologists. SpyTag/SpyCatcher has been widely used for enzyme immobilization, colocalization of different enzymatic activities, and increasing enzyme resilience. Here we present routes and advice for efficient design, expression, and purification of SpyTag/SpyCatcher constructs in bacterial and eukaryotic environments, including the latest 002 variants, and how to analyze reaction efficiency. The SpyInfo webpage collates the different publications and patents using SpyTag/SpyCatcher, while the SpyBank database lists their sequences and expression routes. The ability of SpyTag/SpyCatcher to react in a broad range of situations creates diverse opportunities for augmenting the function of enzymes and other biomolecules., (© 2019 Elsevier Inc. All rights reserved.)

Published
2019
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