RT Journal Article
SR Electronic
T1 SARS-Cov-2 Spike binding to ACE2 is stronger and longer ranged with glycans
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.07.15.452507
DO 10.1101/2021.07.15.452507
A1 Huang, Yihan
A1 Harris, Bradley S.
A1 Minami, Shiaki A.
A1 Jung, Seongwon
A1 Shah, Priya S.
A1 Nandi, Somen
A1 McDonald, Karen A.
A1 Faller, Roland
YR 2021
UL http://biorxiv.org/content/early/2021/07/15/2021.07.15.452507.abstract
AB Highly detailed steered Molecular Dynamics simulations are performed on differently glycosylated receptor binding domains of the SARS-CoV-2 spike protein. The binding strength and the binding range increases with glycosylation. The interaction energy rises very quickly with pulling the proteins apart and only slowly drops at larger distances. We see a catch slip type behavior where interactions during pulling break and are taken over by new interactions forming. The dominant interaction mode are hydrogen bonds but Lennard-Jones and electrostatic interactions are relevant as well.Statement of Significance Glycosylation of the receptor binding domain of the Spike protein of SARS-CoV-2 as well as the ACE2 receptor leads to stronger and longer ranged binding interactions between the proteins. Particularly, at shorter distances the interactions are between residues of the proteins themselves whereas at larger distances these interactions are mediated by the glycans.Competing Interest StatementThe authors have declared no competing interest.