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.  

Why SARS-CoV-2 Spike Mutation D614G has Become the Dominant Variant

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.

University of Michigan - Ann Arbor

S protein amino acid variants

https://doi.org/10.1016/j.cell.2020.06.043

Tracking changes in SARS-CoV-2 Spike: evidence that D614G increases infectivity of the COVID-19 virus

D614G

G614 is a variant of SARS-CoV-2 that is caused by a D614G amino acid change (A-G nucleotide change) in the S protein, which simultaneously also causes C-T mutations in three different areas of the spike

G614

- study on the first 37 fatal cases of SARS-CoV-2 in Wuhan, China revealed that V354F or V470A substitutions of the spike protein showed increased infectivity
- V354F and V470A are known to increase entry of pseudoviruses into cells expressing ACE2
- although this study is limited, it does suggest the challenge of creating novel therapeutics that target ACE2 and spike protein

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