Title : The binding of heparin to spike glycoprotein inhibits SARS-CoV-2 infection by three mechanisms.

Pub. Date : 2022 Feb

PMID : 34929169






5 Functional Relationships(s)
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1 Biochemical experiments corroborated the simulation results, showing that heparin inhibits the furin-mediated cleavage of spike by binding to the S1/S2 site. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
2 In simulations of the closed spike homotrimer, heparin binds the RBD and the N-terminal domain of two adjacent spike subunits and hinders opening. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
3 In simulations of the closed spike homotrimer, heparin binds the RBD and the N-terminal domain of two adjacent spike subunits and hinders opening. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
4 In simulations of open spike conformations, heparin induces stabilization of the hinge region and a change in RBD motion. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
5 Taken together, our results indicate that heparin can inhibit SARS-CoV-2 infection by three mechanisms: by allosterically hindering binding to the host cell receptor, by directly competing with binding to host heparan sulfate proteoglycan co-receptors, and by preventing spike cleavage by furin. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2