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

The Middle East respiratory syndrome coronavirus spike protein is a large trimeric glycoprotein located on the surface of the MERS-CoV virion. It plays a central role in viral entry by mediating attachment to host cells through the S1 subunit, which contains the receptor-binding domain that binds to human DPP4/CD26. The S2 subunit enables membrane fusion through conformational changes triggered by receptor binding and proteolytic cleavage by host enzymes such as furin, TMPRSS2, and cathepsin L. The spike protein is the main target of neutralizing antibodies and is considered the principal antigenic component for vaccine design and therapy. Structural studies reveal dynamic conformations in both receptor-bound and unbound states, reflecting its functional flexibility. Due to its essential role in viral infection and host specificity, the spike protein is a key therapeutic and diagnostic target for MERS-CoV.

Other names

MERS-CoV envelope spike glycoproteinMERS-CoV S glycoproteinMERS S proteinSpike protein (context: MERS-CoV)S protein (context: MERS-CoV)

Blockade of receptor binding (antibodies or peptides targeting receptor-binding domain) Prevention of membrane fusion (peptide inhibitors binding HR regions) Induction of antibody-mediated neutralization