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Human Coronavirus was first identified by Tyrrel and Byone1 in the 1960s. Until recently its pathogenicity was for the most part considered low, occasionally leading to acute upper respiratory infection in infants, young adults, the elderly and immune compromised patients. The emergence of highly pathogenic strains – Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) first reported in 2002, Middle East Respiratory Syndrome (MERS) first reported in 2012 and SARS-CoV-2 the causative agent for COVID-19 – has created an urgent need for expanding our diagnostic capability, the development of therapeutics and vaccines against Coronaviruses.

Scientist world-wide are working to develop effective solutions to the ongoing COVID-19 pandemic. To support the scientific community’s R&D efforts, IBT Bioservices has developed antibodies and antigens to key target candidates.

SARS-CoV-2 structurally consists of the Spike (S), Nucelocapsid (N), Envelope (E) and Membrane (M) proteins. These proteins share high sequence similarity to the corresponding proteins of SARS-CoV, and MERS-CoV2. The glycosylated Spike (S) protein that projects through the viral envelope and the nucleocapsid (N) protein encoded by all coronaviruses are key targets of drug and therapeutic candidates. 

IBT Bioservices offers antibodies that target the C- and N- terminus of the S1 region, the C-terminus of the S2 region of the Spike protein and the receptor binding domain (RBD). The RBD of the S protein that recognizes the ACE2 receptors on host cells is another key determinant of host and cell tropism3,4,5. The N protein which shows high conservation and mutational stability 6  is considered a potentially  advantageous antigen target for a SARS-CoV2 vaccine. The specificity of these affinity purified polyclonal (rabbit) antibodies has been confirmed via Western blot and ELISA. These polyclonal antibodies and antigens are key tools for detection and as control proteins for immunoassays.

At IBT Bioservice we share your goals of bringing new treatments to the market. We offer discovery tools and testing service to help progress your project toward your developmental milestone and securing your next round of funding. To learn more about IBT Bioservices and our offerings visit our website or emails your questions to

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Fig. 1 Survival after challenge with INFV H1N1 A/Pert/261/2009 (Tamiflu-resistant strain). Inoculum 1xLD90=1.0E+05 PFU/mouse
Survival after challenge with INFV H1N1 A/Pert/261/2009 (Tamiflu-resistant strain) 1.0E+05 PFU/mouse
Survival and weight change in BALB/c mice challenged with INFV A/ Texas/36/91 (H1N1) and treated with antiviral Osletamivir Phosphate (Tamiflu)
Lung viral load and Survival (30 % weight loss cut-off) in BALB/c mice challenged with INFV H3N2 A/HK/1/68.

Alpha (UK) – B. 1.1.7 / 501Y.V1

amino acid mutations: del69–70 HV, del144 Y, N501Y, A570D, D614G, P681H, T761I, S982A, D1118H

Beta (South Africa) – B.1.351

amino acid mutations: K417N, E484K, N501Y, D614G, A701V

Gamma (Brazil) – P.1

amino acid mutations: L18F, T20N, P26S, D138Y, R190S, K417T, E484K, N501Y, D614G, H655Y, T1027I

Epsilon (Ca, USA) B.1.427

amino acid mutations: L452R, D614G

SARS-CoV-2 Parental Strain Wild Type (Wuhan)
SARS-CoV-2 D614G Variant

amino acid mutations: D614G

Epsilon (Ca, USA) B.1.429

amino acid mutations: S13I, W152C, L452R, D614G

SARS-CoV-2 Delta Variant

amino acid mutations: L452R, E484Q