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Stabilized Trimeric Spike Protein SARS-CoV-2 (D614G mutant)

Made in CHO cells

Since the beginning of the COVID-19 pandemic in Wuhan, variants of the SARS-CoV-2 virus carrying a mutation in the spike protein at position 614 have largely replaced the original isolate [8]. See 3D model comparison.

Protein modelling has shown that this D614G mutation has a significant influence on the conformation of the trimeric spike. These structural changes in the G614 variant seem to enhance infectivity of virions through improved binding to the ACE2 receptor [4, 10, 15].

In addition, there are reports that antibodies generated against the Wuhan variant of SARS-CoV-2 may not fully protect against D614G [2, 6]. Interestingly, all current vaccines and diagnostic tests have been developed on the basis of the Wuhan isolate.

It is unclear, but not unthinkable that current vaccine candidates will be less effective against viruses carrying the D614G mutation. In addition, current antibody tests may display decreased sensitivity to antibodies against the 614G variant.

We offer the trimeric spike protein with the D to G mutation as well as the 614D ‘Wuhan’ trimeric protein. This makes these proteins ideal for use in comparative studies.

Product datasheet

This product is intended for research use only.

Stabilized Trimeric Spike Protein SARS-CoV-2 (D614G mutant)
Modifications C-terminal Transmembrane region replaced with a trimerization domain and a polyhistidine tag. Two stabilizing proline mutations. Scrambled S1/S2 furin cleavage site. D614G amino acid change.
Isolate (Seq ID) Wuhan-Hu-1 (GenBank: MN908947) with D614G mutation.
Expression system CHOExpressTMcells
Purity > 95 % as determined by SDS-PAGE.
Molecular weight The recombinant SARS-CoV-2 trimeric spike protein consists of 3576 amino acids and predicts a molecular mass of ˜ 400 kDa.
Endotoxin < 1.0 EU per µg protein as determined by the LAL method.
Format Liquid
Reference Wrapp D. et al. Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation. Science 367, 1260–1263 (2020)

Verification of purity and size of the recombinant trimeric SARS-CoV-2 D614G Spike Protein under non-denaturing conditions. Size-exclusion chromatography (SEC) plot with peak at 4.0 minutes, corresponding to a size of ˜ 400kD.

Verification of size and purity and size of trimeric SARS-CoV-2 D614G spike protein under denaturing conditions. 7.5% SDS-PAGE gel with a band corresponding to the size of the spike monomer; ˜ 150 kD.

3-D model of the recombinant trimeric SARS-CoV-2 spike protein and D614G mutant using Swiss-Model – University of Basel online tools

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