tetano
Editor, Senior Moderator
Nat Commun
. 2020 Nov 26;11(1):6013.
doi: 10.1038/s41467-020-19808-4.
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Lizhou Zhang[SUP] 1 [/SUP], Cody B Jackson[SUP] 1 [/SUP], Huihui Mou[SUP] 1 [/SUP], Amrita Ojha[SUP] 1 [/SUP], Haiyong Peng[SUP] 1 [/SUP], Brian D Quinlan[SUP] 1 [/SUP], Erumbi S Rangarajan[SUP] 2 [/SUP], Andi Pan[SUP] 1 [/SUP], Abigail Vanderheiden[SUP] 3 4 5 6 [/SUP], Mehul S Suthar[SUP] 3 4 5 6 [/SUP], Wenhui Li[SUP] 7 [/SUP], Tina Izard[SUP] 2 [/SUP], Christoph Rader[SUP] 1 [/SUP], Michael Farzan[SUP] 8 [/SUP], Hyeryun Choe[SUP] 9 [/SUP]
Affiliations
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.
. 2020 Nov 26;11(1):6013.
doi: 10.1038/s41467-020-19808-4.
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Lizhou Zhang[SUP] 1 [/SUP], Cody B Jackson[SUP] 1 [/SUP], Huihui Mou[SUP] 1 [/SUP], Amrita Ojha[SUP] 1 [/SUP], Haiyong Peng[SUP] 1 [/SUP], Brian D Quinlan[SUP] 1 [/SUP], Erumbi S Rangarajan[SUP] 2 [/SUP], Andi Pan[SUP] 1 [/SUP], Abigail Vanderheiden[SUP] 3 4 5 6 [/SUP], Mehul S Suthar[SUP] 3 4 5 6 [/SUP], Wenhui Li[SUP] 7 [/SUP], Tina Izard[SUP] 2 [/SUP], Christoph Rader[SUP] 1 [/SUP], Michael Farzan[SUP] 8 [/SUP], Hyeryun Choe[SUP] 9 [/SUP]
Affiliations
- PMID: 33243994
- DOI: 10.1038/s41467-020-19808-4
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.