Abstract
An outbreak of SARS-CoV-2 coronavirus (COVID-19) first detected in Wuhan, China, has created a public health emergency all over the world. The pandemic has caused more than 340 million confirmed cases and 5.57 million deaths as of 23 January 2022. Although carbohydrates have been found to play a role in coronavirus binding and infection, the role of cell surface glycans in SARS-CoV-2 infection and pathogenesis is still not understood. Herein, we report that the SARS-CoV-2 spike protein S1 subunit binds specifically to blood group A and B antigens, and that the spike protein S2 subunit has a binding preference for Lea antigens. Further examination of the binding preference for different types of red blood cells (RBCs) indicated that the spike protein S1 subunit preferentially binds with blood group A RBCs, whereas the spike protein S2 subunit prefers to interact with blood group Lea RBCs. Angiotensin converting enzyme 2 (ACE2), a known target of SARS-CoV-2 spike proteins, was identified to be a blood group A antigen-containing glycoprotein. Additionally, 6-sulfo N-acetyllactosamine was found to inhibit the binding of the spike protein S1 subunit with blood group A RBCs and reduce the interaction between the spike protein S1 subunit and ACE2.
Highlights
Since emerging from Wuhan, China in January 2020, the SARS-CoV-2 coronavirus has widely spread around the globe [1]
The results showed that SARS-CoV-2 spike proteins interacted with several glycans, including blood group antigens, which was coherent with the binding with groups A and B human red blood cells (RBCs)
Our results suggested that the specific carbohydrate modifications on Angiotensin converting enzyme 2 (ACE2) might be responsible for its binding to SARSCoV-2 spike protein S1 subunit
Summary
Since emerging from Wuhan, China in January 2020, the SARS-CoV-2 coronavirus has widely spread around the globe [1]. The densely glycosylated spike (S) protein of SARS-CoV-2, a trimeric class I fusion protein with a metastable prefusion conformation [2,3], docks to enter host cells. When binding to a host-cell receptor, the S1 subunit triggers a dramatic structural rearrangement to fuse the viral membrane with the host-cell membrane, leading to receptor-dependent endocytosis [4,5]. These interactions destabilize the prefusion trimer and result in shedding of the S1 subunit and the transition of the S2 subunit into a stable postfusion conformation [6]
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