The SARS-CoV-2 spike (S)-protein D614G mutation is now globally predominant. This study compares the properties of the mutated S protein (sG614) with the original (sD614), finding that pseudoviruses carrying S614G enter ACE2-expressing cells more efficiently. This increased entry correlates with less S1-domain shedding and higher S-protein incorporation into the virion. Similar results were obtained with virus-like particles. However, D614G did not alter S-protein binding to ACE2 or neutralization sensitivity. The increased infectivity is likely due to increased functional S protein incorporation into the virion.

Lizhou Zhang, Cody B. Jackson, Huihui Mou, Amrita Ojha, Haiyong Peng, Brian D. Quinlan, Erumbi S. Rangarajan, Andi Pan, Abigail Vanderheiden, Mehul S. Suthar, Wenhui Lio, Tina Izard, Christoph Rader, Michael Farzan, Hyeryun Choe