Alternative names:
SARS-CoV-2 Alpha variant

Data and images for Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)

Figures

Figure 1

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Cell-based spike protein binding assay.
Schematic overview illustrating how our biotinylated spike proteins can be applied to analyze binding to ACE2-expressing cells.

Figure 1

Cell-based spike protein binding assay.
Schematic overview illustrating how our biotinylated spike proteins can be applied to analyze binding to ACE2-expressing cells.

Figure 2

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Results of the cell-based binding assay using biotinylated
Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK).
ACE2-expressing cells (Vero E6 cells) were incubated with biotinylated SARS-CoV-2 spike monomer of the wild-type, Wuhan variant (Recombinant SARS-CoV-2 Spike-Prot (HEK)-Biotin), B.1.1.7, Alpha (Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)-Biotin) and B.1.351, Beta (Recombinant SARS-CoV-2 Spike-Prot B.1.351 (HEK)-Biotin).
Different protein concentrations were used, and ACE2-bound spike protein was subsequently detected by fluorescent staining with streptavidin-PE. Quantification of stained cells at different protein concentrations illustrates that Miltenyi Biotec's recombinant spike monomers are biologically functional and show a titratable, high-affinity binding to cell surface ACE2. B.1.1.7 (HEK) displayed the highest binding affinity to ACE2.

Figure 2

Results of the cell-based binding assay using biotinylated
Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK).
ACE2-expressing cells (Vero E6 cells) were incubated with biotinylated SARS-CoV-2 spike monomer of the wild-type, Wuhan variant (Recombinant SARS-CoV-2 Spike-Prot (HEK)-Biotin), B.1.1.7, Alpha (Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)-Biotin) and B.1.351, Beta (Recombinant SARS-CoV-2 Spike-Prot B.1.351 (HEK)-Biotin).
Different protein concentrations were used, and ACE2-bound spike protein was subsequently detected by fluorescent staining with streptavidin-PE. Quantification of stained cells at different protein concentrations illustrates that Miltenyi Biotec's recombinant spike monomers are biologically functional and show a titratable, high-affinity binding to cell surface ACE2. B.1.1.7 (HEK) displayed the highest binding affinity to ACE2.

Figure 3

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SDS-PAGE of biotinylated Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)
under reduced (R) and non-reduced (NR) conditions.

Figure 3

SDS-PAGE of biotinylated Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)
under reduced (R) and non-reduced (NR) conditions.

Specifications for Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)

Overview

The SARS-CoV-2 spike glycoprotein (S) mediates the entry of the virus into target cells via its interaction with the angiotensinconverting enzyme 2 (ACE2) receptor, thereby initiating the infection. It forms a homotrimeric structure on the surface of the SARS-CoV-2 virus and represents the major target for diagnostic and therapeutic agents. The ectodomain of the S glycoprotein comprises the N-terminal S1 subunit, including the receptor binding domain (RBD) and the C-terminal S2 subunit. The ectodomain spans from aa12 to aa1213 followed by a transmembrane helix beginning at aa1214–aa1234. The C-terminus of the native protein is formed by a cytoplasmic domain spanning aa1235–aa1273.
The SARS-CoV-2 mutant strain B.1.1.7 also known as Alpha variant or variant of concern (VOC 202012/01), was first identified in the United Kingdom in September 2020. Due to increased transmissibility it spread rapidly around the globe. The B.1.1.7 lineage (Alpha variant) differs from the wild type sequence by 23 amino acid mutations: 14 non-synonymous mutations, 3 deletions and 6 synonymous mutations. One of these mutations leads to an amino acid substitution (N501Y) in the RBD of the B.1.1.7 lineage (Alpha variant), which mainly contributes to the increased infectivity of B.1.1.7 as mutations in the RBD affect antibody recognition and ACE2 binding efficiency. The N501Y mutation also emerged independently in SARS-CoV-2 variants in the B.1.351 lineage (Beta variant) and P.1 linage (Gamma variant).
The Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK) protein covers the ectodomain of the viral surface protein including amino acids V16 to K1211. It was engineered to contain the stabilizing proline substitutions at position K986P and V987P. The native sequence of the Furin cleavage site (RRAR at residues 682–685) was substituted by GSAS to further increase recombinant protein stability.
In addition, the SARS-CoV-2 Spike-Prot B.1.1.7 (HEK) protein contains the amino acid deletions Δ69, Δ70 and Δ144, as well as the amino acid substitutions N501Y, A570D, D614G, P681H, T716I, S982A, and D1118H. The protein is extended at its C-terminus with a His-tag and an AviTag™. Recombinant SARS-CoV-2 Spike-Prot B.1.1.7 (HEK)-Biotin is specifically biotinylated at a single site, preserving full functionality of the protein.

Alternative names

SARS-CoV-2 Alpha variant

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