The D614G mutation in SARS-CoV-2 has become the dominant variant of the virus over the course of the pandemic.  To investigate more fully as to why the D614G mutation has become dominant, researchers developed a cell line capable of inducing ACE2 expression to expose to D614G versus the wild type.     
- The D614G mutated variant is able to more efficiently enter cells, because it can enter across a wider range of ACE2 levels than the wild type.
- Viral incorporation of D614G variant protomers is higher than that of the wild type.
- The D614G variant exhibits a higher trimerization efficiency, meaning that it is preferentially incorporated into trimers than the wild type.  

Johns Hopkins University

D614G is an amino acid in the S protein that was originally the most dominant variant of SARS-CoV-2. Located on the surface of the S protein protomer, D614G is responsible for forming a hydrogen bond with a neighboring promoter, which brings together the S1 subunit of a protomer with the S2 subunit of another protomer.

D614G

Michaud, W. A., Boland, G. M., & Rabi, S. A. (2020). The SARS-CoV-2 Spike mutation D614G increases entry fitness across a range of ACE2 levels, directly outcompetes the wild type, and is preferentially incorporated into trimers. BioRxiv, 2020.08.25.267500. https://doi.org/10.1101/2020.08.25.267500


The SARS-CoV-2 Spike mutation D614G increases entry fitness across a range of ACE2 levels, directly outcompetes the wild type, and is preferentially incorporated into trimers

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