Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Accessible Surface Glycopeptide Motifs on Spike Glycoprotein of 2019-nCoV: Implications on Vaccination and Antibody Therapeutics

Version 1 : Received: 24 February 2020 / Approved: 25 February 2020 / Online: 25 February 2020 (13:44:15 CET)
Version 2 : Received: 12 April 2020 / Approved: 13 April 2020 / Online: 13 April 2020 (11:09:29 CEST)

How to cite: Zhou, D.; Qi, R.; Zhang, W. Accessible Surface Glycopeptide Motifs on Spike Glycoprotein of 2019-nCoV: Implications on Vaccination and Antibody Therapeutics. Preprints 2020, 2020020381. https://doi.org/10.20944/preprints202002.0381.v1 Zhou, D.; Qi, R.; Zhang, W. Accessible Surface Glycopeptide Motifs on Spike Glycoprotein of 2019-nCoV: Implications on Vaccination and Antibody Therapeutics. Preprints 2020, 2020020381. https://doi.org/10.20944/preprints202002.0381.v1

Abstract

Corona viruses hijack human enzymes to assembly sugar coat on Spike glycoproteins. The mechanism that human antibodies may uncover the antigenic viral peptide epitopes hidden by sugar coat are unknown. In this study, we analyzed the high-resolution Cryo-EM structure of Spike glycoproteins. The results showed that electron densities of glycans cover most of the SARS-CoV Spike receptor binding domain except FSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQ. The glycosylated 2019-nCoV Spike protein by homology structure modeling showed a similar exposed sequence YQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQ. Other surface-exposed domains included those located on Central Helix, between amino acids 967 and 1016 of SARS-CoV, and 985 to 1034 of 2019-nCoV Spike protein. As the majority of antibody paratopes bind to peptide portion with or without sugar modification, we propose a snake-catcher model that a minimal length of peptide is first clamped by a paratope, and the binding is either strengthened by sugars close to peptide, or not interfered by sugar modification.

Keywords

2019-nCoV; corona virus; glycopeptide; N-linked glycans; antibody; cryo-EM structure; crystal structures; epitope prediction

Subject

Medicine and Pharmacology, Medicine and Pharmacology

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.