19 Oct.: Seminar with Sebastian Jaksch on "Timescales of Cell Membrane Fusion Mediated by SARS- CoV2 Spike Protein and its Receptor ACE2"


On Thursday, 19 October at 15:15 hrs, Dr. Sebastian Jaksch will hold a seminar at the Ångström Laboratory in room Å90102.

Dr. Jaksch is a soft-matter physicist who work at the intersection between physics, chemistry and biology. Among other things he work on instrumentation and neutron scattering, building the small-angle neutron scattering SANS instrument SKADI at the upcoming ESS and a novel high-flux capable high-resolution neutron detector SoNDe.


"We investigated the SARS- CoV2 membrane fusion timescale by means of small-angle neutron scattering (SANS) using hydrogen/deuterium contrast variation. After the successful production of virus-like vesicles and human- host-cell-like vesicles we were able to follow the fusion of the respective vesicles in real-time. This was done using deuterated and protonated phospholipids in the vesicles in a neutron-contrast matched solvent. The vesicles were identical apart from either the presence or absence of the SARS-CoV2 spike protein. The human host-cell-like vesicles were carrying an ACE2 receptor protein in all cases. In case of the absence of the spike protein a fusion over several hours was observed in agreement with literature, with a time constant of 4.5 h. In comparison, there was not time evolution, but immediate fusion of the vesicles when the spike protein was present. Those two figures, fusion over several hours and fusion below 10 s corresponding to the absence or presence of the spike protein allow an upper-limit estimate for the fusion times of virus-like vesicles with the SARS-CoV2 spike protein of 10 s. This very fast fusion, when compared to the case without spike protein it is a factor of 2500, can also help to explain why infection with SARS-CoV2 can be so effective and fast. Studying spike protein variants using our method may explain differences in transmissibility between SARS-CoV2 strains. In addition, the model developed here can potentially be applied to any enveloped virus."

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