Middle East respiratory syndrome coronavirus (MERS-CoV), a novel
coronavirus linked to severe respiratory tract illness, was initially identified in 2012.
Since then, 1401 individuals have been infected with this virus in 26 countries, with
543 people (39%) dying. Severe respiratory infection, sometimes accompanying shock,
acute renal damage, and coagulopathy are all symptoms of these disorders. This
pandemic has sparked worldwide worry because of its human-to-human transmission
via intimate contact. The Eastern Province, Riyadh, and Makkah were severely hit. In
2014, the pandemic progressed fastest in Makkah, Riyadh, and Eastern Province in
2013. Effective therapeutic and immunological solutions based on solid molecular
research were critical, with the threat of an epidemic looming. The MERS-CoV
intrinsic genetic heterogeneity across different clades may have set the way for crossspecies transmission and alterations in inter-species and intra-species tropism. Host
protease blockers include transmembrane serine protease 2 (TMPRSS2), cathepsin L,
and furin. According to sequence comparison and modeling research, the viral spike
features a putative receptor-binding domain (RBD) that enables this interaction.2.
The dipeptidyl-peptidase 4 (DPP4)-propeller engages with the receptor-binding
subdomain but not the intrinsic hydrolase domain. The receptor binding subdomain of
MERS CoV and severe acute respiratory syndrome coronavirus (SARS CoV) is
drastically different. This chapter aims to explain the genetic architecture of host
proteins involved in MERS-CoV and compare it with other coronaviruses.
Keywords: MERS-CoV, Protein S, Adaptive immune response, LY6E protein, DPP4, Dipeptidyl peptidase 4, CD26 protein.
