@article{BaeckerKochEibenetal.2017,
  author    = {B{\"a}cker, Matthias and Koch, Claudia and Eiben, Sabine and Geiger, Fania and Eber, Fabian and Gliemann, Hartmut and Poghossian, Arshak and Wege, Christina and Sch{\"o}ning, Michael Josef},
  title     = {Tobacco mosaic virus as enzyme nanocarrier for electrochemical biosensors},
  series = {Sensors and Actuators B: Chemical},
  volume    = {238},
  journal   = {Sensors and Actuators B: Chemical},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2016.07.096},
  pages     = {716 -- 722},
  year      = {2017},
  abstract  = {The conjunction of (bio-)chemical recognition elements with nanoscale biological building blocks such as virus particles is considered as a very promising strategy for the creation of biohybrids opening novel opportunities for label-free biosensing. This work presents a new approach for the development of biosensors using tobacco mosaic virus (TMV) nanotubes or coat proteins (CPs) as enzyme nanocarriers. Sensor chips combining an array of Pt electrodes loaded with glucose oxidase (GOD)-modified TMV nanotubes or CP aggregates were used for amperometric detection of glucose as a model system for the first time. The presence of TMV nanotubes or CPs on the sensor surface allows binding of a high amount of precisely positioned enzymes without substantial loss of their activity, and may also ensure accessibility of their active centers for analyte molecules. Specific and efficient immobilization of streptavidin-conjugated GOD ([SA]-GOD) complexes on biotinylated TMV nanotubes or CPs was achieved via bioaffinity binding. These layouts were tested in parallel with glucose sensors with adsorptively immobilized [SA]-GOD, as well as [SA]-GOD crosslinked with glutardialdehyde, and came out to exhibit superior sensor performance. The achieved results underline a great potential of an integration of virus/biomolecule hybrids with electronic transducers for future applications in biosensorics and biochips.},
  language  = {en}
}
@article{KochPoghossianSchoeningetal.2018,
  author    = {Koch, Claudia and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Wege, Christian},
  title     = {Penicillin Detection by Tobacco Mosaic Virus-Assisted Colorimetric Biosensors},
  series = {Nanotheranostics},
  volume    = {2},
  journal   = {Nanotheranostics},
  number    = {2},
  publisher = {Ivyspring},
  address   = {Sydney},
  issn      = {2206-7418},
  doi       = {10.7150/ntno.22114},
  pages     = {184 -- 196},
  year      = {2018},
  abstract  = {The presentation of enzymes on viral scaffolds has beneficial effects such as an increased enzyme loading and a prolonged reusability in comparison to conventional immobilization platforms. Here, we used modified tobacco mosaic virus (TMV) nanorods as enzyme carriers in penicillin G detection for the first time. Penicillinase enzymes were conjugated with streptavidin and coupled to TMV rods by use of a bifunctional biotin-linker. Penicillinase-decorated TMV particles were characterized extensively in halochromic dye-based biosensing. Acidometric analyte detection was performed with bromcresol purple as pH indicator and spectrophotometry. The TMV-assisted sensors exhibited increased enzyme loading and strongly improved reusability, and higher analysis rates compared to layouts without viral adapters. They extended the half-life of the sensors from 4 - 6 days to 5 weeks and thus allowed an at least 8-fold longer use of the sensors. Using a commercial budget-priced penicillinase preparation, a detection limit of 100 µM penicillin was obtained. Initial experiments also indicate that the system may be transferred to label-free detection layouts.},
  language  = {en}
}
@article{PoghossianJablonskiKochetal.2018,
  author    = {Poghossian, Arshak and Jablonski, Melanie and Koch, Claudia and Bronder, Thomas and Rolka, David and Wege, Christina and Sch{\"o}ning, Michael Josef},
  title     = {Field-effect biosensor using virus particles as scaffolds for enzyme immobilization},
  series = {Biosensors and Bioelectronics},
  volume    = {110},
  journal   = {Biosensors and Bioelectronics},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0956-5663},
  doi       = {10.1016/j.bios.2018.03.036},
  pages     = {168 -- 174},
  year      = {2018},
  abstract  = {A field-effect biosensor employing tobacco mosaic virus (TMV) particles as scaffolds for enzyme immobilization is presented. Nanotubular TMV scaffolds allow a dense immobilization of precisely positioned enzymes with retained activity. To demonstrate feasibility of this new strategy, a penicillin sensor has been developed by coupling a penicillinase with virus particles as a model system. The developed field-effect penicillin biosensor consists of an Al-p-Si-SiO₂-Ta₂O₅-TMV structure and has been electrochemically characterized in buffer solutions containing different concentrations of penicillin G. In addition, the morphology of the biosensor surface with virus particles was characterized by scanning electron microscopy and atomic force microscopy methods. The sensors possessed a high penicillin sensitivity of ~ 92 mV/dec in a nearly-linear range from 0.1 mM to 10 mM, and a low detection limit of about 50 µM. The long-term stability of the penicillin biosensor was periodically tested over a time period of about one year without any significant loss of sensitivity. The biosensor has also been successfully applied for penicillin detection in bovine milk samples.},
  language  = {en}
}
@article{WendlandtKochBritzetal.2023,
  author    = {Wendlandt, Tim and Koch, Claudia and Britz, Beate and Liedek, Anke and Schmidt, Nora and Werner, Stefan and Gleba, Yuri and Vahidpour, Farnoosh and Welden, Melanie and Poghossian, Arshak and Sch{\"o}ning, Michael Josef},
  title     = {Facile Purification and Use of Tobamoviral Nanocarriers for Antibody-Mediated Display of a Two-Enzyme System},
  series = {Viruses},
  volume    = {9},
  journal   = {Viruses},
  number    = {15},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1999-4915},
  doi       = {doi.org/10.3390/v15091951},
  pages     = {Artikel 1951},
  year      = {2023},
  abstract  = {Immunosorbent turnip vein clearing virus (TVCV) particles displaying the IgG-binding domains D and E of Staphylococcus aureus protein A (PA) on every coat protein (CP) subunit (TVCVPA) were purified from plants via optimized and new protocols. The latter used polyethylene glycol (PEG) raw precipitates, from which virions were selectively re-solubilized in reverse PEG concentration gradients. This procedure improved the integrity of both TVCVPA and the wild-type subgroup 3 tobamovirus. TVCVPA could be loaded with more than 500 IgGs per virion, which mediated the immunocapture of fluorescent dyes, GFP, and active enzymes. Bi-enzyme ensembles of cooperating glucose oxidase and horseradish peroxidase were tethered together on the TVCVPA carriers via a single antibody type, with one enzyme conjugated chemically to its Fc region, and the other one bound as a target, yielding synthetic multi-enzyme complexes. In microtiter plates, the TVCVPA-displayed sugar-sensing system possessed a considerably increased reusability upon repeated testing, compared to the IgG-bound enzyme pair in the absence of the virus. A high coverage of the viral adapters was also achieved on Ta2O5 sensor chip surfaces coated with a polyelectrolyte interlayer, as a prerequisite for durable TVCVPA-assisted electrochemical biosensing via modularly IgG-assembled sensor enzymes.},
  language  = {en}
}