M. Dieterle, D. Haslwanter, R. Bortz, A. S. Wirchnianski, G. Lasso, O. Vergnolle, Shawn A Abbasi, J. Fels, E. Laudermilch, C. Florez, A. Mengotto, D. Kimmel, R. Malonis, G. Georgiev, J. Quiroz, J. Barnhill, L. Pirofski, J. Daily, J. Dye, J. Lai, A. Herbert, K. Chandran, R. Jangra
Cell Host & Microbe, 2020
Summary There is an urgent need for vaccines and therapeutics to prevent and treat COVID-19. Rapid SARS-CoV-2 countermeasure development is contingent on the availability of robust, scalable, and readily deployable surrogate viral assays to screen antiviral humoral responses, define correlates of immune protection, and down-select candidate antivirals. Here, we generate a highly infectious recombinant vesicular stomatitis virus (VSV) bearing the SARS-CoV-2 spike glycoprotein S as its sole entry glycoprotein and show that this recombinant virus, rVSV-SARS-CoV-2 S, closely resembles SARS-CoV-2 in its entry-related properties. The neutralizing activities of a large panel of COVID-19 convalescent sera can be assessed in a high-throughput fluorescent reporter assay with rVSV-SARS-CoV-2 S, and neutralization of rVSV-SARS-CoV-2 S and authentic SARS-CoV-2 by spike-specific antibodies in these antisera is highly correlated. Our findings underscore the utility of rVSV-SARS-CoV-2 S for the development of spike-specific therapeutics and for mechanistic studies of viral entry and its inhibition.
Cited by 27 publications.
Field of study: Biology