Zbiotech’s heparan sulfate glycan array helps researchers identify the sugar substrates of SARS-CoV-2.

SARS-CoV-2 infects human cells by interacting with heparan sulfate proteoglycans with its spike glycoprotein, and it helps viral particles recognize the ACE2 receptor to enter the host cells. Chittum and colleagues investigated the bindings of recombinant S1 and RBD proteins to various heparan sulfate glycans. They aimed to decipher the selectivity of heparan sulfate recognition by SARS-CoV-2 spike glycoprotein and hoped to find potential heparan sulfate or heparan sulfate-like antagonists. If the selective heparan sulfate–binding domain is identified, it could potentially discover novel sugar-based antiviral agents.

To identify the heparan sulfate glycans to which the S1 and RBD proteins bind, researchers used our heparan sulfate glycan array, which includes 24 heparan sulfate glycans varying in length and sulfate content. S1 and RBD proteins had similar affinities for 8 different heparan sulfate glycans, and these results were confirmed by dual-filter computational studies afterward. These findings helped researchers identify the heparan sulfate–binding domain and used this structural information for a virtual screening of a library of >93 000 carbohydrate sequences.

Our heparan sulfate glycan array helped scientists examine the fine-tuned binding interactions between viral proteins and their sugar substrates. It generated valuable structural insights into the sugar-receptor interaction, which led to reconstructing the receptor binding domain for large-scale virtual drug screening.