COVID-19 Breakthrough:  Full-length (1273-aa) trimeric coronavirus spike protein expressed in E. coli bacteria

Versatile Biosciences, LLC is the world’s first laboratory to successfully express the full-length of the coronavirus spike protein (Accession: YP_009724390), both stably and efficiently in E. coli. Our T4 phage technology maintains stable characteristics across generations and lends to large scale production. This is in contrast with current protein expression via eukaryotic cells (e.g. HEK-293 and CHO cells), where it is difficult to obtain a stable cell strain carrying such large proteins with multi-generational cell propagation, and therefore challenging to produce large scale amounts of full-length spike protein.

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Innovation Significance

• Our innovative method should better support more effective mass production of spike protein when compared to existing methods. Further, we can produce any desired sequence for the development of protein-based and/or T4 bacteriophage nanometer particles as carrier vaccines. 

• E Coli. expressed full-length spike antigen shows opportunities to utilize special unique humanizing B cell strain for humanized antibody production as a therapeutic drug(s) for serious SARS-CoV-2 patients. 

• This method can be used to produce very large proteins for biomedical use.

• Less expensive spike glycoproteins for COVID-19 immune diagnosis reagents.
   

It is paramount that vaccines become safer, more effective, and more easily modified to address emerging variants. Our discovery should assist the innovators of the world to meet this challenge.

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This novel achievement was headed by VersatileBio’s Principal Scientist, Dr. Zhaojun Ren, whereby he constructed an innovative T4:T7 Hybrid-Phage expression vector and leveraged to express the SARS-CoV-2 full length in 3822-bp, 1273-aa (with 6×His tag) spike protein. The protein was supplied in its native state as a Trimer (3 x 158 kDa) and verified via high-resolution tandem mass spectrometry. Please click HERE for more technical details.

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Further technical details:

• Conformation is identical to the membrane bound trimeric spike protein on the viral env​elope.

• Single span transmembrane protein (aa 1 - 1273) 

• Furin cleavage site RRAR mutated to GSAS.

• Supplied in its native state as a Trimer (3 x 158 kDa)

• Expressed in E. coli cells.

• N-terminal 6His tag for affinity purification

• Solubilization and stabilization in PBS

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