SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity

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<jats:title>Abstract</jats:title><jats:p>SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S<jats:sup>G614</jats:sup>) with the original (S<jats:sup>D614</jats:sup>). We report here pseudoviruses carrying S<jats:sup>G614</jats:sup> enter ACE2-expressing cells more efficiently than those with S<jats:sup>D614</jats: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.</jats:p>

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  • Nature Communications

    Nature Communications 11 (1), 6013-, 2020-11-26

    Springer Science and Business Media LLC

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