Fluidity One-M

Emmenegger et al. from the University Hospital Zurich, report that serum antibodies against the wild-type, delta, and omicron variants of SARS-CoV-2 have similar affinity, indicating a broad cross-clade immune response. Changes in antibody titers were primarily driven by B-cell expansion, rather than affinity maturation, after infection or vaccination.

Professor Adriano Aguzzi, University Hospital Zurich commented: “[MDS] is the breakthrough that gives us invaluable new insights and could be a game-changer for our ability to understand, diagnose, and treat COVID-19.”

In this collaboration with the University of Graz, the MAffCon Assay was used to measure the binding of trastuzumab (Herceptin) to HER2 extracted from breast cancer cells, with consistent results to literature values and the potential for straightforward quantification of HER2 expression.

Lena Bauernhofer, Institute of Molecular Biosciences, University of Graz, Austria commented: “The improvement using MDS comes from the fact that we can produce this robust and precise data without much purification.”

Linse et al., Nature Struct. Mol. Biol., 2020, 27, 1125-1133. DOl: 10.1038/41594-020-0505-6

Linse et al. combine kinetic analyses with MDS binding measurements to address the mechanism of action of four clinical stage anti-AB antibodies. They quantify the influence of these antibodies on the aggregation kinetics and on the production of oligomeric aggregates and link these effects to the affinity and stoichiometry of each antibody for monomeric and fibrillar forms of AB. Their results reveal that, only one of these four antibodies dramatically reduces the flux of AB oligomers which is linked to its inhibitory potential.