Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein.

ABSTRACT: Middle East respiratory syndrome coronavirus (MERS-CoV) targets the epithelial cells of the respiratory tract both in humans and in its natural host, the dromedary camel. Virion attachment to host cells is mediated by 20-nm-long homotrimers of spike envelope protein S. The N-terminal subunit of each S protomer, called S1, folds into four distinct domains designated S1^A through S1^D Binding of MERS-CoV to the cell surface entry receptor dipeptidyl peptidase 4 (DPP4) occurs via S1^B We now demonstrate that in addition to DPP4, MERS-CoV binds to sialic acid (Sia). Initially demonstrated by hemagglutination assay with human erythrocytes and intact virus, MERS-CoV Sia-binding activity was assigned to S subdomain S1^A When multivalently displayed on nanop

SUBMITTER: Li W 

PROVIDER: S-EPMC5635925 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature