PT  - JOURNAL ARTICLE
AU  - Huang, Yihan
AU  - Harris, Bradley S.
AU  - Minami, Shiaki A.
AU  - Jung, Seongwon
AU  - Shah, Priya S.
AU  - Nandi, Somen
AU  - McDonald, Karen A.
AU  - Faller, Roland
TI  - SARS-Cov-2 Spike binding to ACE2 is stronger and longer ranged with glycans
AID  - 10.1101/2021.07.15.452507
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.07.15.452507
4099  - http://biorxiv.org/content/early/2021/07/15/2021.07.15.452507.short
4100  - http://biorxiv.org/content/early/2021/07/15/2021.07.15.452507.full
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.