Title : SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2.

Pub. Date : 2020 Nov 12

PMID : 32970989






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
2 Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
3 Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
4 Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2
5 Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus. Heparin surface glycoprotein Severe acute respiratory syndrome coronavirus 2