SARS-CoV-2 S glycoprotein (V367F, HEK293, His)

SARS-CoV-2 S glycoprotein (V367F, HEK 293, His) is a SARS-CoV-2 S glycoprotein V367F protein with a His-flag. SARS-CoV-2 S glycoprotein (V367F) is a SARS-CoV-2 variant carrying the S protein amino acid (aa) change V367F. The mutant type V367F continuously circulating worldwide displays higher binding affinity to human ACE2 ^[1].

SARS-CoV-2, causes the global pandemic coronavirus disease 2019 (Covid-19). SARS-CoV-2 belongs to a family of viruses known as coronaviruse. SARS-CoV-2 is the third human coronavirus this century known to cause pneumonia with a significant case-fatality rate.
SARS-CoV-2 is comprised of four structural proteins: Spike protein (S protein), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N).
D614G does not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 is reduced due to a faster dissociation rate^[2][3].

Virus

HEK293

C-10*His

P0DTC2 (R319-F541, V367F)

43740568  [NCBI]

RVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSFLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF

Approximately 27.9 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.

• [1]. Junxian Ou, et al. V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity. J Virol. 2021 Jul 26;95(16):e0061721.  [Content Brief]

  [2]. Leonid Yurkovetskiy, et al. Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant. Cell. 2020 Oct 29;183(3):739-751.e8.  [Content Brief]

  [3]. Jessica A Plante, et al. Spike mutation D614G alters SARS-CoV-2 fitness. Nature. 2021 Apr;592(7852):116-121.  [Content Brief]