Recombinant Human coronavirus 229E (HCoV-229E) Surface glycoprotein (S) (785-873 aa) [His/Myc-Tag], E. coli

Recombinant Human coronavirus 229E (HCoV-229E) Surface glycoprotein (785-873 aa) was expressed in E. coli with a 10xHis-tag at the N-terminus and a Myc-tag at the C-terminus. The biological activity was determined by its binding ability in a functional ELISA. This product can be used in ELISA, WB, IP.

Human coronavirus 229E (HCoV-229E)

785-873 aa

DVLQENQKILAASFNKAMTNIVDAFTGVNDAITQTSQALQTVATALNKIQDVVNQQGNSLNHLTSQLRQNFQAISSSIQAIYDRLDTIQ

10xHis-tag at the N-terminus and Myc-tag at the C-terminus

17.2 kDa

>90%, determined by SDS-PAGE.

Unconjugated

S

Surface glycoprotein

S1 region attaches the virion to the cell membrane by interacting with host ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.

S glycoprotein; E2; Peplomer protein; S