Large-scale analysis of SARS-CoV-2 spike-glycoprotein mutants demonstrates the need for continuous screening of virus isolates

Within the last year, a few infections with the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) quickly turned into the global COVID-19 pandemic infecting and threatening death for millions of people all over the globe. The viral spike protein is responsible for viral binding and entry to host cells and thus mediates infection. Hence, the protein is also of particular interest and the major target for recently approved mRNA vaccines or neutralizing antibodies.
In this study, Barbara Schrörs and her colleagues gathered 147,413 genomic assemblies and 2,393 NGS sequencing datasets to detect non-synonymous spike protein mutations and infer their frequency within a given sample and the effect on potential antibody binding sites and known T cell epitopes. They confirm a low mutation rate, but also discovered an increase of mutation rates of the spike protein over time. In addition, some of the discovered mutations might have an effect on antibody binding or T-cell recognition and thus have an impact on the efficacy of current or upcoming vaccines.
The authors conclude that the results demonstrate the increasing importance of monitoring SARS-CoV-2 sequences for an early detection of variants that require adaptations in preventive and therapeutic strategies.

The study was published as a pre-print in BioRxiv (

[Image: SARS-CoV-2 spike-glycoprotein (PDB:]