| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-66 |
Sentence |
denotes |
SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2. |
| T2 |
67-235 |
Sentence |
denotes |
We show that SARS-CoV-2 spike protein interacts with both cellular heparan sulfate and angiotensin-converting enzyme 2 (ACE2) through its receptor-binding domain (RBD). |
| T3 |
236-333 |
Sentence |
denotes |
Docking studies suggest a heparin/heparan sulfate-binding site adjacent to the ACE2-binding site. |
| T4 |
334-473 |
Sentence |
denotes |
Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold. |
| T5 |
474-592 |
Sentence |
denotes |
Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2. |
| T6 |
593-666 |
Sentence |
denotes |
On cells, spike protein binding depends on both heparan sulfate and ACE2. |
| T7 |
667-865 |
Sentence |
denotes |
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. |
| T8 |
866-991 |
Sentence |
denotes |
We suggest a model in which viral attachment and infection involves heparan sulfate-dependent enhancement of binding to ACE2. |
| T9 |
992-1116 |
Sentence |
denotes |
Manipulation of heparan sulfate or inhibition of viral adhesion by exogenous heparin presents new therapeutic opportunities. |
