Protein aggregation

Find the perfect BMG LABTECH plate reader for your virology research.

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.

    • Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers

      Werner, TER;Bernson, D;Esbjörner, EK;Rocha, S;Wittung-Stafshede, P;[2020]

      Proc Natl Acad Sci U S A

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    • Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability

      Pradhan, T;Annamalai, K;Sarkar, R;Huhn, S;Hegenbart, U;Schönland, S;Fändrich, M;Reif, B;[2020]

      J Biol Chem

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    • TDP-43 and Tau Oligomers in Alzheimer\'s Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia

      Montalbano, M;McAllen, S;Cascio, FL;Sengupta, U;Garcia, S;Bhatt, N;Ellsworth, A;Heidelman, EA;Johnson, OD;Doskocil, S;Kayed, R;[2020]

      Neurobiol Dis

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    • Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates

      Sneideris, T;Ziaunys, M;Chu, BK;Chen, RP;Smirnovas, V;[2020]

      Int J Mol Sci

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    • Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

      Linse, S;Scheidt, T;Bernfur, K;Vendruscolo, M;Dobson, CM;Cohen, SIA;Sileikis, E;Lundqvist, M;Qian, F;O'Malley, T;Bussiere, T;Weinreb, PH;Xu, CK;Meisl, G;Devenish, SRA;Knowles, TPJ;Hansson, O;[2020]

      Nat Struct Mol Biol

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