Affiliations
- State Key Laboratory of Virology, Institute for Vaccine Research and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan, 430072, Hubei Province, China.
- Anhui Zhifei Longcom Biopharmaceutical, Hefei, China.
- State Key Laboratory of Virology, Institute for Vaccine Research and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan, 430072, Hubei Province, China. huanyan@whu.edu.cn.
- State Key Laboratory of Virology, Institute for Vaccine Research and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan, 430072, Hubei Province, China; Hubei Province key Laboratory of Allergy and Immunology, Wuhan University, Wuhan, 430072, Hubei Province, China. sunhui@whu.edu.cn.
PMID: 37709229 DOI: 10.1016/j.ijbiomac.2023.126874
Abstract
Background: The SARS-CoV-2 spike protein receptor-binding domain (RBD) is a key target for neutralizing antibodies and vaccines. However, the RBD's glycoforms affect neutralization and immunogenicity.
Methods: Deglycosylated versions of ZF2001 were created to evaluate binding affinity and neutralization. Various glycosylation modifications (removal of sialic acid, O-glycans, N-glycans) were assessed.
Results: Complex glycosylation enhanced the vaccine's humoral immunogenicity and antigen presentation by forming more hydrogen bonds with MHC-II molecules.
Conclusion: The study highlights the impact of RBD glycosylation on vaccine design and production.
Keywords
Glycosylation; Immunogenicity; Immunoreactivity; Vaccine; ZF2001.
