Viruses are equally a threat to plants, bacteria, animals, and humans. They use their hosts to reproduce and can thereby damage them. This can lead, for example, to crop or farm animal losses and pandemics. On the other hand, viruses serve as tools for genetic engineering and the targeted modification of genomes.
Modern virology characterises viruses molecularly and functionally and uses this information to develop diagnostic tests, antiviral drugs and vaccines. Traditionally, virology largely relied on microscopic methods. Nowadays, microplate-based assays increase throughput and enable the measurement of replication, virus neutralization, binding of molecules to viral particles and much more.
Virus assays range from simple ELISA assays for measuring antibody titer to live-cell assays to measure replication. The variety of virus assays in combination with the need for cell-based methods requires a flexible microplate reader.
The CLARIOstar®Plus microplate reader offers this flexibility. It is a modular multi-mode reader that can be equipped with fluorescence, luminescence, absorbance and advanced detection modes. With its Atmospheric Control Unit, it is further optimized for live-cell assays as it creates the optimal environment for long-term cell-based experiments. The CLARIOstar Plus can be equipped with a red-shifted PMT for increased sensitivity with fluorophores emitting in the red range of light. These are often used in cell assays to avoid autofluorescence.
The PHERAstar FSX multi-mode microplate reader is the ideal platform for screening departments, where potential anti-viral compounds have to be detected quickly and efficiently in high throughput. In addition, it can quickly and effortlessly measure all FRET, TR-FRET and fluorescence polarization dual emission assays. These are often used in binding/interaction assays for anti-viral compound screens.
Browse our Resources section for information about specific applications, literature citations, videos, blog articles and many other publications. Many of the resources provided are associated with current and previous instrument models and versions.
Dual Channel Kinetic assays for detecting ligand bias at GPCRsPaul Tewson (1) , Scott Martinka (1) , Kevin M. Harlen (1) , Thom Hughes (1) , Anne Marie Quinn (1) , Sam R.J. Hoare (2) , Carl Peters (3), (1) Montana Molecular, Bozeman, MT , (2) Pharmechanics, Owego, NY , (3) BMG LABTECH Inc., NC, USA, 11/2019
Analyze binding kinetics with HTRFNicolas Pierre , Thomas Roux, Cisbio Bioassays, Codolet, France, 05/2019
Fluorescence polarization-based RNA synthesis assayStefan Reich , Stephen Cusack, European Molecular Biology Laboratory, 10/2018
NanoBRET™ assay quantitatively evaluates VEGF binding to the VEGFR2 in real-time in living cellsKilpatrick LE (1) , Friedman-Ohana R (2) , Alcobia DC (1) , Riching K (2) , Peach CJ (1) , Wheal AJ (1) , Briddon SJ (1) , Robers MB (2) , Zimmerman K (2) , Machleidt T (2) , Wood KV (2) , Woolard J (1) , Hill SJ (1), (1) Division of Physiology, Pharmacology and Neuroscience, University of Nottingham, UK , (2) Promega Corporation, Madison, WI, USA, 01/2018
CRISPR/Cas9 genome-edited cells express nanoBRET-donor that monitors protein interaction and traffickingCarl White (1,2) , Ethan See (1,2) , Kevin Pfleger (1,2,3), (1) Molecular Endocrinology and Pharmacology, Harry Perkins Institute of Medical Research, Australia , (2) Centre for Medical Research, The University of Western Australia, Australia , (3) Dimerix Limited, Nedlands, Australia, 01/2018
8-Benzylaminoxanthine scaffold variations for selective ligands acting on adenosine A2A receptors. Design, synthesis and biological evaluationRead article
Adenosine A2A and A3 Receptors Are Able to Interact with Each Other. A Further Piece in the Puzzle of Adenosine Receptor-Mediated SignalingRead article
Int J Mol Sci
New Insights into Arrestin Recruitment to GPCRsRead article
Int J Mol Sci
Serosurveillance and Molecular Investigation of Wild Deer in Australia Reveals Seroprevalence of Pestivirus InfectionRead article
Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2Read article
Nat. Struct. Mol. Biol.