Middle East respiratory syndrome-related coronavirus spike protein (MERS-CoV S protein) (MERS-CoV S protein)

The Middle East respiratory syndrome-related coronavirus spike protein (MERS-CoV S) is a large, type I transmembrane glycoprotein that forms homotrimers on the viral surface, giving the virus its characteristic crown-like appearance (UniProt, 2024). It is the primary determinant of viral host range and tissue tropism, functioning by mediating attachment to the host cell receptor, dipeptidyl peptidase 4 (DPP4), and subsequent fusion of the viral and cellular membranes (PubMed, 2013). The protein is proteolytically cleaved into two subunits: S1, which contains the receptor-binding domain (RBD), and S2, which contains the fusion machinery (NIH, 2023). As the principal target for neutralizing antibodies, the MERS-CoV spike protein is the central focus for the development of vaccines and therapeutic monoclonal antibodies (Nature, 2019). Drugs targeting this protein typically aim to block the RBD-DPP4 interaction or prevent the structural rearrangements of the S2 subunit necessary for infection (PubMed, 2020). Therapeutic candidates include monoclonal antibodies like REGN3048 and REGN3051, which bind specifically to the RBD to prevent viral entry (Regeneron, 2020). Understanding its structure and function is critical for addressing the high mortality rate associated with MERS-CoV infections (WHO, 2023).

Other names

Spike glycoproteinS proteinMERS-CoV SPeplomer proteinSurface glycoprotein

Neutralization of viral entry by blocking the interaction between the viral receptor-binding domain (RBD) and the host cell receptor dipeptidyl peptidase 4 (DPP4), or by inhibiting the conformational changes required for membrane fusion (PubMed, 2020).