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7 Oct 2021

SARS-CoV-2 peptides and antibodies from CRB

The Covid-19 pandemic has caused widespread disruption around the world with around 195 million confirmed infections globally to date. Here at Cambridge Research Biochemicals (CRB) we have been supporting the phenomenal effort within the research community to characterise and study this new coronavirus as quickly and thoroughly as possible. We have added a range of new products targeted at the causal pathogen SARS-CoV-2 available on our discovery peptides and discovery antibodies websites.

The SARS-CoV-2’s RNA genome encodes four essential structural proteins: the membrane protein (M), the envelope protein (E), the nucleocapsid protein (N) and the spike glycoprotein (S). CRB has produced a range of peptides from the multi-functional N protein. The N protein is involved in the formation of the helical nucleocaspid structure (which stores the RNA within the virion), the facilitation of virion assembly, and increasing the transcription efficiency of the virus.

SARS-CoV-2 Spike or S protein is of particular interest due to various aspects of its biology and its multiple functions, for this reason CRB have raised an antibody against a region of the SARS-CoV-2 S protein as well as offering a peptide. S is a transmembrane protein which gives the virus its distinctive “corona” or crown-like appearance. The ectodomain of S protein is divided into two subunits, S1 and S2. S1 helps in host receptor binding and contains the receptor-binding domain (RBD)/receptor binding motif (RBM). The RBD of the S1 subunit has a superior capacity to induce neutralising antibodies and mediate T-cell responses, therefore current Covid-19 vaccines are designed around the S protein.

S protein is essential for viral entry into the cell, mediated via binding to the angiotensin-converting enzyme 2 (ACE2) receptor on the host, to which CRB have also raised a polyclonal antibody. ACE2 is highly expressed in lungs, nasal epithelium, intestine, kidney, endothelium and heart. The binding of SARS-CoV-2 with ACE2 also leads to an imbalance in the renin-angiotensin system (RAS) which can result in the exacerbation of pneumonia symptoms. After virus entry viral genome RNA is translated into two polyproteins, pp1a and pp1ab, these undergo autoproteolytic cleavage by main protease (MPro) and 3C-like protease (3CLpro) to produce mature non-structural proteins essential for replication and synthesis of more viral RNA.

Infection with SARS-CoV-2 can cause disease ranging from asymptomatic or mild to severe diseases including death. In severe cases, high levels of inflammatory proteins including: IFNα, IFNγ, IL-1β, IL-6, IL-12, IL-18, IL-33, TNFα, TGFβ, CCL2, CCL3, CCL5, CXCL8, CXCL9, CXCL10, are released, encouraging a “cytokine storm” which leads to the excessive inflammation. This exaggerated immune response can lead to damage to host tissues which remains one of the key challenges in fighting this viral pathogen.

See our full range of SARS-CoV-2 related peptides here

See our SARS-CoV-2 and ACE2 antibodies here

References:

Dhama et al., (2020). Coronavirus Disease 2019–COVID-19. Clin Microbiol Rev33(4): e00028-20. PMID: 32580969

Gheblawi et al., (2020). Angiotensin-Converting Enzyme 2: SARS-CoV-2 Receptor and Regulator of the Renin-Angiotensin System. Circ Res126(10): PMID: 32264791

O’Leary et al., (2021). Unpacking Pandora from Its Box: Deciphering the Molecular Basis of the SARS-CoV-2 Coronavirus. Int J Mol Sci. 22(1): 386. PMID: 33396557