<i>O</i>-GalNAc glycosylation affects the immunogenicity of the receptor-binding domain (RBD) of SARS-CoV-2 spike protein-Reference-Cited by-同舟云学术

O-GalNAc glycosylation affects the immunogenicity of the receptor-binding domain (RBD) of SARS-CoV-2 spike protein

Published:2023 Issue:13 Volume:59 Page:1797-1800
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Rong Yongheng¹,Wang Xingyun²,Mao Weian¹,Chen Min¹^ORCID,Wang Shengjun³,Wang Peng George²^ORCID,He Yunjiao²,Kong Yun¹^ORCID

Affiliation:

1. National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, China

2. School of Medicine, Southern University of Science and Technology, Shenzhen, 518055, China

3. School of Health and Life Sciences, University of Health and Rehabilitation Sciences, Qingdao 266071, China

Abstract

Herein, O-GalNAc glycosylated RBD (Tn-RBD) was synthesized as antigen via in vitro glycosylation reactions. The inhibition ability against hACE2 binding of antibodies induced with Tn-RBD was 30–40% increased.

Funder

Key Technology Research and Development Program of Shandong

National Natural Science Foundation of China

Shandong University

Shenzhen Municipal Science and Technology Innovation Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CC/D2CC06583E

Reference22 articles.

1. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China

2. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

3. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

4. Structural basis of receptor recognition by SARS-CoV-2

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