Proteomics

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Impact of Glycosylation on the SARS-CoV-2 Recombinant RBD Vaccine

ABSTRACT: Comparative analysis was performed at both nucleic acid and protein vaccine levels to provides a reference for the "glycosylation quality control" of SARS-CoV-2 RBD vaccines. For instance, monitoring the glycoform distribution at the N343 site (e.g., ensuring the proportion of the M5 glycoform is ≥30%) can help maintain the structural stability of the vaccine antigen and the consistency of its immunogenicity. Additionally, the findings regarding the characterization of various glycosylation sites can offer a solution to the longstanding challenge of difficult horizontal comparison among different recombinant SARSCoV- 2 RBD protein vaccines.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): B Cell

DISEASE(S): Acute Leukemia

SUBMITTER: Tie Gao  

LAB HEAD: Tie Gao

PROVIDER: PXD076685 | Pride | 2026-06-08

REPOSITORIES: Pride

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Investigating the effects and underlying mechanisms of glycosylation sites on the immunogenicity of COVID-19 vaccines.

Wang Heru H   Li Xiang X   He Peng P   Yang Sen S   Liu Xiaoya X   Zhu Qianhui Q   Liu Pan P   Fang Xin X   Wang Chenfei C   Bi Ying Y   Jiang Gaojian G   Sun Yufei Y   Chen Hongxu H   Gao Tie T   Luo Ji J   Rong Huan H   Liu Xiaosa X   Wang Xiangxi X   Zhang Yuxia Y   Hu Zhongyu Z  

Signal transduction and targeted therapy 20260513 1

Glycosylation plays a pivotal role in modulating the structure and immunogenicity of viral antigens. Three glycosylation sites on the receptor-binding domain (RBD) of SARS-CoV-2, including N331, N343 (N-linked), and T323 (O-linked), are highly conserved and remain unchanged across multiple variant strains. To investigate their functional relevance, a series of site-directed glycosylation-deficient mutants were generated on the basis of the RBD-dimer antigen of the ZF2001 vaccine (developed by ZF  ...[more]

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