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

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O-GalNAc glycosylation affects the immunogenicity of the receptor-binding domain (RBD) of SARS-CoV-2 spike protein
Chemical Communications ( IF 4.3 ) Pub Date : 2023-01-16 , DOI: 10.1039/d2cc06583e
Yongheng Rong ₁ , Xingyun Wang ₂ , Weian Mao ₁ , Min Chen ₁ , Shengjun Wang ₃ , Peng George Wang ₂ , Yunjiao He ₂ , Yun Kong ₁

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The spike protein of SARS-CoV-2 has been widely used as an effective vaccine immunogen, although some limitations still remain. Herein, O-GalNAc glycosylated RBD (Tn-RBD) was synthesized as an antigen via in vitro glycosylation reactions. The inhibition ability against hACE2 binding of antibodies induced with Tn-RBD was 30–40% increased compared to that induced with RBD. This result implies that Tn-glycosylation might play important roles in the immunogenicity of the RBD protein, which should be considered in the design of novel vaccines to fight against COVID-19.

中文翻译：

O-GalNAc 糖基化影响 SARS-CoV-2 刺突蛋白受体结合域 (RBD) 的免疫原性

SARS-CoV-2 的刺突蛋白已被广泛用作有效的疫苗免疫原，但仍存在一些局限性。在此，O -GalNAc 糖基化 RBD (Tn-RBD)通过体外糖基化反应合成为抗原。与用 RBD 诱导的抗体相比，用 Tn-RBD 诱导的抗体对 hACE2 结合的抑制能力增加了 30-40%。这一结果表明 Tn-糖基化可能在 RBD 蛋白的免疫原性中发挥重要作用，在设计抗 COVID-19 的新型疫苗时应考虑这一点。

更新日期：2023-01-16

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