Recently, Prof. Ping WANG’s group at School of Chemistry and Chemical Engineering of Shanghai Jiao Tong University published an article titled Synthetic Homogeneous Glycoforms of the SARS-CoV-2 Spike Receptor-Binding Domain Reveals Different Binding Profiles of Monoclonal Antibodies on Angewandte Chemie International Edition. (https://onlinelibrary.wiley.com/doi/10.1002/anie.202100543)


Wang’s group used the state-of-the-art union of oligo-saccharide, peptide and protein chemistry to develop a flexible and robust means to construct six structurally defined glycosylated RBDs bearing defined structure glycoforms at T323, N331, and N343 efficiently. S-RBD is one of the most complex glycosylated proteins synthesized so far. The plasma resonance results showed that the size of RBD glycosylation had no significant impact on its binding to ACE2. Binding tests with clinically approved neutralizing antibodies (S309, CB6, etc.) have shown that the immune escape effect caused by viral glycosylation is not significant if the antibody target is a non-glycosylated region. Under selective pressure, the evolution of a virus might result in glycoforms and glycosylation site alteration. Moreover, the platform represents a versatile strategy for accessing synthetic glycosylated RBDs that could be relevant for other virus studies, including the SAR study of different RBD glycoforms, and verifying the capacity of mAbs for other pathogens such as SARS and MERS.

This work was also supported by Prof. Biao YU and Prof. Jing WANG at Shanghai institute of Organic Chemistry at Chinese Academy of Sciences, and Prof. Tianlei YING at Fu Dan University.

Translator: Chenyun SUN