SARS-CoV-2 RBD Proteins (501Y.V1/V2/V3) for COVID Variants of
UK, South Africa, and Brazil
Product | Cat. No. | Variant | Mutations | Source |
---|---|---|---|---|
SARS-CoV-2 (COVID-19) S RBD (N501Y) Protein | 11-064 | UK 501Y.V1 | N501Y | Mammalian |
SARS-CoV-2 (COVID-19) S RBD (K417N, E48K, N501Y) Protein | 11-065 | South Africa 501Y.V2 | K417N, E48K, N501Y | Mammalian Cells |
SARS-CoV-2 (COVID-19) S RBD (E484K, K417T, N501Y) Protein | 11-066 | Brazil 501Y.V3 | E484K, K417T, N501Y | Mammalian Cells |
SARS-CoV-2 (COVID-19) S RBD (E484K) Protein | 11-067 | 501Y.V2/V3 | E484K | Mammalian |
SARS-CoV-2 (COVID-19) Spike (D614G) Trimer Protein | 92-748 | 501Y.V2 | D614G | Human Cells |
SARS-CoV-2 (COVID-19) Spike (D614G) S1 Protein | 92-746 | 501Y.V2 | D614G | Human Cells |
B.1.1.7 Lineage of SARS-CoV-2 (2019-nCoV)
In September of 2020 a new lineage of SARS-CoV-2, known as B.1.1.7, was discovered in the United Kingdom. This lineage was found to have developed 14 lineage-specific amino acid replacements and 3 deletions prior to its discovery. It appears that the B.1.1.7 is now evolving at a rate similar to other SARS-CoV-2 lineages which have a rate of mutation of about one to two mutations per month (Duchene et al. 2020).
One of the mutations associated with this lineage is a N501Y in the spike protein of the virus. It is believed that this mutation is able to increase the spike protein's affinity for the host ACE2 receptor (Starr et al. 2020) and it has been associated with increased infectivity and virulence (Gu et al. 2020). B.1.1.7 viruses have also been shown to have a P681H mutation in the cleavage site of spike protein. This location is one of the residues that make up the furin cleavage site between S1 and S2 in spike. The S1/S2 furin cleavage site has been shown in animal models to promote viral entry into respiratory epithelial cells and transmission (Hoffmann et al. 2020; Peacock et al. 2020; Zhu et al. 2020). The spike proteins of this lineage has also been shown to have a deletion at amino acids 69-70. This mutation in the receptor binding domain of spike is a recurrent deletion that has been found in various lineages associated with SARS-CoV-2 (McCarthy et al. 2020; Kemp et al. 2020). Outside of spike, a Q27 stop mutation truncates the ORF8 protein of the virus, rendering the protein inactive. An ORF8 deletion at amino acid 382 has a mild effect on virus replication in human airway cells (Gamage et al. 2020). The B.1.1.7. lineage also has five synonymous mutations in ORF1ab and one synonymous mutation in the M gene.
ProSci Inc. has developed specific antibodies with the peptide immunogen including the mutation site and these antibodies can be used for Western Blot, ELISA, IHC/IF, and other immunoassays. |
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Non-synonymous mutations and deletions of B.1.1.7 lineage.
Gene | Nucleotide | Amino Acid | Protein | Related ProSci Abs | Ab Immunogen | Biological Significance |
---|---|---|---|---|---|---|
Spike | 21765-21770 deletion | HV 69-70 deletion | (S1-NT) | Recurrent deletions in vairous lineages related to several RBD mutations | ||
A23063T | N501Y | RBD | 9087 | Mutation site included | An increase in the binding affinity of ACE2 receptor and enhance infectivity and virulence | |
C23604A | P681H | S1-CT | 9091/9095 | Mutation site included | Promote viral entry into human cells and transmission in animal models | |
21991-21993 | Y144 deletion | S1 | ||||
C23271A | A570D | S1 | ||||
C23709T | T716I | S2-NT | ||||
T24506G | S982A | S2' | ||||
G24914C | D1118H | S2' | ||||
ORF1ab | C3267T | T1001I | NSP3/PL-PRO | |||
C5388A | A1708D | NSP3/PL-PRO | ||||
T6954C | I2230T | NSP3/PL-PRO | ||||
11288-11296 deletion | SGF 3675-3677 deletion | NSP6 | ||||
ORF8 | C27972T | Q27stop | ORF8-NT | Slight effect on virus replication in human cells with deletions | ||
G28048T | R52I | ORF8 | Incoming ORF8 Ab | Mutation site included | ||
A28111G | Y73C | ORF8 | 10-511 | Mutation site included | ||
N | 28280 GAT-CTA | D3L | N-NT | 35-579 | Mutation site included | |
C28977T | S235F | N |
[Edited from Rambaut et al, 2020]
SARS-CoV-2 Spike Recombinant Proteins (D614G)
Product | Cat. No. | Source | Fusion Tag | Sequence |
---|---|---|---|---|
SARS-CoV-2 (COVID-19) S-Trimer Protein Recombinant Protein (D614G) | 92-748 | Human Cells | C-6 His Tag | Cys15 - Gln1208 (D614G) |
SARS-CoV-2 (COVID-19) S1 Protein Recombinant Protein (D614G) | 92-746 | Human Cells | C-10 His Tag | Gln14 - Arg685 (D614G) |
SARS-CoV-2 (COVID-19) S RBD Mutant Recombinant Proteins
Product | Cat. No. | Source | Fusion Tag | Sequence |
---|---|---|---|---|
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-750 | Human Cells | C-6His Tag | Arg319 - Phe541 (F342L) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-751 | Human Cells | C-6His Tag | Arg319 - Phe541 (N354D) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-752 | Human Cells | C-6His Tag | Arg319 - Phe541 (V367F) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-753 | Human Cells | C-6His Tag | Arg319 - Phe541 (R408I) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-754 | Human Cells | C-6His Tag | Arg319 - Phe541 (A435S) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-755 | Human Cells | C-6His Tag | Arg319 - Phe541 (K458R) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-756 | Human Cells | C-6His Tag | Arg319 - Phe541 (G476S) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-757 | Human Cells | C-6His Tag | Arg319 - Phe541 (V483A) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-758 | Human Cells | C-6His Tag | Arg319 - Phe541 (D364Y) |
SARS-CoV-2 (COVID-19) Spike RBD Recombinant Protein | 92-759 | Human Cells | C-6His Tag | Arg319 - Phe541 (V341I) |
SARS-CoV-2 (COVID-19) S RBD-SD1 Recombinant Protein (V367F) | 92-742 | Human Cells | C-6 His Tag | Arg319 - Ser591 (V367F) |
SARS-CoV-2 (COVID-19) Spike RBD-SD1 Recombinant Protein (N354D, D364Y) | 92-743 | Human Cells | C-6His Tag | Arg319 - Ser591 (N354D, D364Y) |
SARS-CoV-2 (COVID-19) Spike RBD-SD1 Recombinant Protein (W436R) | 92-744 | Human Cells | C-6His Tag | Arg319 - Ser591 (W436R) |
SARS-CoV-2 (COVID-19, 2019-nCoV) Research
Duchene, Sebastian, Leo Featherstone, Melina Haritopoulou-Sinanidou, Andrew Rambaut, Philippe Lemey, and Guy Baele. 2020. “Temporal Signal and the Phylodynamic Threshold of SARS-CoV-2.” Virus Evolution 6 (2): veaa061.
Gamage, Akshamal M., Kai Sen Tan, Wharton O. Y. Chan, Jing Liu, Chee Wah Tan, Yew Kwang Ong, Mark Thong, et al. 2020. “Infection of Human Nasal Epithelial Cells with SARS-CoV-2 and a 382-Nt Deletion Isolate Lacking ORF8 Reveals Similar Viral Kinetics and Host Transcriptional Profiles.” PLoS Pathogens 16 (12): e1009130.
Gu, Hongjing, Qi Chen, Guan Yang, Lei He, Hang Fan, Yong-Qiang Deng, Yanxiao Wang, et al. 2020. “Adaptation of SARS-CoV-2 in BALB/c Mice for Testing Vaccine Efficacy.” Science 369 (6511): 1603–7.
Hoffmann, Markus, Hannah Kleine-Weber, and Stefan Pöhlmann. 2020. “A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells.” Molecular Cell 78 (4): 779–84.e5.
Kemp, S. A., D. A. Collier, R. Datir, S. Gayed, A. Jahun, M. Hosmillo, Iatm Ferreira, et al. 2020. “Neutralising Antibodies Drive Spike Mediated SARS-CoV-2 Evasion.” Infectious Diseases (except HIV/AIDS). medRxiv. https://doi.org/10.1101/2020.12.05.20241927.
McCarthy, Kevin R., Linda J. Rennick, Sham Nambulli, Lindsey R. Robinson-McCarthy, William G. Bain, Ghady Haidar, and W. Paul Duprex. 2020. “Natural Deletions in the SARS-CoV-2 Spike Glycoprotein Drive Antibody Escape.” Microbiology. bioRxiv.
Peacock, Thomas P., Daniel H. Goldhill, Jie Zhou, Laury Baillon, Rebecca Frise, Olivia C. Swann, Ruthiran Kugathasan, et al. 2020. “The Furin Cleavage Site of SARS-CoV-2 Spike Protein Is a Key Determinant for Transmission due to Enhanced Replication in Airway Cells.” Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.09.30.318311.
Starr, Tyler N., Allison J. Greaney, Sarah K. Hilton, Daniel Ellis, Katharine H. D. Crawford, Adam S. Dingens, Mary Jane Navarro, et al. 2020. “Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding.” Cell 182 (5): 1295–1310.e20.
Zhu, Yunkai, Fei Feng, Gaowei Hu, Yuyan Wang, Yin Yu, Yuanfei Zhu, Wei Xu, et al. 2020. “The S1/S2 Boundary of SARS-CoV-2 Spike Protein Modulates Cell Entry Pathways and Transmission.” Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.08.25.266775.