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By screening hundreds of artificial antibodies, researchers at Karolinska Institutet in Sweden and EMBL Hamburg in Germany have identified an antibody that may prevent the new coronavirus from infecting human cells.
The analysis, which is printed in the journal Nature Communications, also reveals how electrons can be quickly generated in the event of future pandemics.
On the surface of SARS-CoV-2 are spike proteins that provide coronaviruses their characteristic look and help them to infect cells.
These proteins utilize their three finger-like projections, known as receptor-binding domain names, to bind to the surface protein ACE2 on human cells.
Antibodies that prevent the spike proteins from binding to the host cell can thus block SARS-CoV-2 disease.
Fragments of antibodies, known as nanobodies, that occur naturally in camelidae, have been produced to stop SARS-CoV-2 from entering cells, but the development process is relatively time consuming.
Eearch group has been working closely with Ben Murrell’s and Gerald McInerney’s groups at KI and Christian Löw’s group at EMBL Hamburg in Germany to find sybodies able to block SARS-CoV-2 infection utilizing a newly developed technical platform.
In a collaboration between EMBL Hamburg and Karolinska Institutet, we’ve managed to develop nanobodies, so-called sybodies, which are not only tiny but also extremely stable and relatively simple and cheap to produce.”
Martin Hällberg, Researcher, Department of Cell and Molecular Biology, Karolinska Institute
They found that a few of the hundreds of synthetic antibodies produced, especially one called Sybody 23, proved extremely effective in blocking the binding process between the viral spike proteins and the human surface protein ACE2.
The researchers then used electron cryomicroscopy (cryo-EM) at KI’s recently opened 3D-EM facility to gain an understanding of how the artificial nanobody blocks SARS-CoV-2 by specifying the structure of the spike proteins bound to Sybody 23.
The spike protein finger-like projections can be either”up” when binding to ACE2 or”down” when hiding from the human immune system.
The structural studies showed that Sybody 23 binds to these two states, effectively blocking the regions where the binding process would normally take place on ACE2. The studies also showed that spike proteins bound to Sybody 23 adopt two different conformations.
This structural insight will make it easier for the researchers to design mixtures of sybodies able to bind to various regions of the SARS-CoV-2 virus’s spike proteins.
They hope then to be able to enhance the efficacy of the antibodies and make it harder for the virus to prevent neutralisation by mutating.
“We show that the use of synthetic antibody libraries combined with structural studies presents great opportunities to rapidly create efficacious therapeutic antibodies, which could also be useful against new viruses in a future pandemic,” says Dr Hällberg.
Karolinska Institute
Custódio, T. F., et al. (2020) Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2. Nature Communications. doi.org/10.1038/s41467-020-19204-y.
