The newly-emerging Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe and fatal acute respiratory disease in humans. Despite global efforts, the potential for an associated pandemic in the future cannot be excluded. Since September 2012, 1,368 laboratory-confirmed cases of human infection by the Middle East respiratory syndrome coronavirus (MERS-CoV) have officially been reported to World Health Organization as of 17 July 2015, including at least 490 related deaths with a fatality rate of ~35.8%.

MERS-CoV belongs to the beta-genus and uses human dipeptidyl peptidase 4 (DPP4) as its host receptor. Receptor recognition is a major determinant of coronavirus host range and tropism. An envelope-anchored trimeric spike protein is responsible for coronavirus entry into host cells via binding to the host receptor and subsequently fusing viral and host membranes. The spike protein consists of a receptor-binding S1 subunit and a membrane fusion S2 subunit. The S1 subunit consists of an N-terminal and a C-terminal domain, both of which can function as receptor-binding domains (RBD). However, it is the C-domain that interacts with DPP4.

This entry represents the core-subdomain of the RBD which is a five-stranded antiparallel beta-sheet with several short alpha-helices.

PMID:23903833 PMID:26391698