Description |
MERS Spike protein trimer (R748A, R751A, V1060P, L1061P), His Tag (SPN-M52H5) is expressed from human 293 cells (HEK293). It contains AA Tyr 18 - Trp 1295 (Accession # K0BRG7 (R748A, R751A, V1060P, L1061P)). The recombinant protein has a T4 fibritin trimerization motif. Proline substitutions (V1060P, L1061P) and alanine substitutions (R748A, R751A) are introduced to stabilize the trimeric prefusion state of MERS-CoV Spike protein and abolish the furin cleavage site, respectively. |
Background |
The MERS or Middle East Respiratory Syndrome Coronavirus, is a member of the coronavirus family and is known to cause severe respiratory illness in humans. The MERS protein is a type I transmembrane protein that plays a vital role in the virus's ability to infect host cells. It is composed of three main domains: the extracellular domain, the transmembrane domain, and the cytoplasmic domain. The extracellular domain, further divided into S1 and S2 subunits, is responsible for receptor recognition and binding. The S1 subunit contains the Receptor Binding Domain (RBD), which is crucial for the virus's attachment to and entry into host cells. The RBD specifically interacts with the host cell receptor, facilitating the initial step of infection. The S2 subunit, on the other hand, is responsible for membrane fusion. It contains a fusion peptide that inserts into the host cell membrane, initiating the fusion process. This fusion allows the virus's genetic material to be released into the host cell, initiating the infection process. |