MERS-CoV Research Reagents — Anti-MERS-CoV Antibodies & Proteins for Diagnostics & Vaccine Development

Middle East Respiratory Syndrome (MERS) is a severe respiratory illness caused by MERS-CoV, a lineage C betacoronavirus (genus Merbecovirus, family Coronaviridae) first identified in 2012 in Saudi Arabia. MERS-CoV is primarily transmitted from infected camels to humans, with limited human-to-human transmission predominantly occurring in healthcare settings. As of 2024, confirmed cases have been reported across the Arabian Peninsula, with sporadic outbreaks in the Republic of Korea and other regions. The case fatality rate averages 34%, with higher mortality in elderly and immunocompromised populations. The single-stranded positive-sense RNA genome (~30 kb) encodes the structural spike glycoprotein (S), the nucleocapsid protein (N), membrane protein (M), and envelope protein (E), along with multiple non-structural proteins. No specific antiviral therapies or approved vaccines are currently available, making diagnostic development and therapeutic antibody research critical priorities.

Research Use Only (RUO)Not intended for diagnostic or therapeutic procedures.

MERS-CoV virion structure and key research targets — Spike glycoprotein, nucleocapsid, membrane and envelope proteins, and host immune response

Fig. 1 MERS-CoV structure and infection pathway. Spike (S) glycoprotein mediates receptor binding and cell entry; N protein encapsidates the genome. Key research targets highlighted in orange.

abinScience provides recombinant antibodies, polyclonal antibodies, InVivoMAb functional-grade antibodies, and recombinant proteins for key MERS-CoV research targets. Products are validated for ELISA, WB, IHC, IF, neutralization, and SPR. All manufactured by our parent company AtaGenix Laboratories under ISO 9001 & ISO 13485 quality systems. Contact us for custom antibody development.

Key Research Targets

Spike (S) Glycoprotein — The S protein is the primary virion surface antigen responsible for receptor binding and cell entry via human dipeptidyl peptidase-4 (hDPP-4). The S protein is cleaved into two functional subunits: S1 (receptor-binding domain) and S2 (fusion peptide and transmembrane anchor). S is the dominant target for neutralizing antibodies and the primary vaccine candidate antigen. Anti-S antibodies support neutralization assays, receptor-binding inhibition studies, vaccine immunogenicity evaluation, and conformational epitope mapping. InVivoMAb-grade anti-S enables passive immunization and protective efficacy studies in animal models.
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Nucleocapsid (N) Protein — N protein encapsidates the 30 kb positive-sense RNA genome and is the most abundantly expressed viral protein during infection. N is highly immunogenic and undergoes early seroconversion, making it the primary diagnostic antigen in MERS-CoV serological assays (IgM/IgG ELISA, immunofluorescence). Anti-N antibodies and recombinant N proteins support rapid diagnostic ELISA development, IHC-based tissue detection, and viral replication quantification studies.
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Membrane (M) Protein — M protein is a transmembrane glycoprotein essential for virion assembly and budding. It interacts with other structural proteins (S, E, N) during virion maturation and plays a role in immune evasion through interference with host interferon signaling. Anti-M antibodies enable structural studies of virion assembly, immunofluorescence detection, and investigation of M-mediated innate immune antagonism in infected cells.
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Envelope (E) Protein — E protein is a small transmembrane viroporin with ion-channel activity that facilitates viral assembly and host cell membrane permeabilization. E protein acts as a major immunodominant epitope and antagonizes host innate immunity. Anti-E antibodies support functional studies of viroporin activity, visualization of infected cell morphology via immunofluorescence, and mechanistic studies of coronavirus-induced cell lysis and immune evasion.
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References

1. Zaki AM, van Boheemen S, Bestebroer TM, et al. Isolation of a novel coronavirus from a man with pneumonia in Saudi Arabia. N Engl J Med. 2012;367(19):1814-1820. DOI

2. Wang N, Shi X, Jiang L, et al. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell Res. 2013;23(8):986-993. DOI

3. Donaldson EF, Haskew AN, Gates JE, et al. Recombinant MERS-CoV expressing a patch-tag is attenuated in vitro and remains pathogenic in vivo. Virology. 2014;452-453:152-159. DOI

4. Falzarano D, de Wit E, Rasmussen AL, et al. Treatment with interferon-alpha2b and ribavirin improves outcome in MERS-CoV-infected rhesus macaques. Nat Med. 2013;19(10):1313-1317. DOI