SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 33243994.
- Also identified by DOI 10.1038/s41467-020-19808-4 and PMC identifier 7693302.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S<sup>G614</sup>) with the original (S<sup>D614</sup>). We report here pseudoviruses carrying S<sup>G614</sup> enter ACE2-expressing cells more efficiently than those with S<sup>D614</sup>. This increased entry correlates with less S1-domain shedding and higher S-protein incorporation into the virion. Similar results are obtained with virus-like particles produced with SARS-CoV-2 M, N, E, and S proteins. However, D614G does not alter S-protein binding to ACE2 or neutralization sensitivity of pseudoviruses. Thus, D614G may increase infectivity by assembling more functional S protein into the virion.
Medical subject headings
- COVID-19
- SARS-CoV-2
- Spike Glycoprotein, Coronavirus
- Virion
- Virus Assembly
- Virus Internalization