Recombinant SARS-CoV-2 S Protein Binds to Glycans of the Lactosamine Family in vitro

---

Alexandr B. Ryzhikov¹, Galina S. Onkhonova¹, Ilnaz R. Imatdinov¹, Elena V. Gavrilova¹, Rinat A. Maksyutov¹, Elena A. Gordeeva², Galina V. Pazynina², Ivan M. Ryzhov², Nadezhda V. Shilova^2,3, and Nicolai V. Bovin^2,a*

¹Vector State Research Center of Virology and Biotechnology, Rospotrebnadzor, 630559 Koltsovo, Novosibirsk Region, Russia

²Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia

³Kulakov National Medical Research Center for Obstetrics, Gynecology and Perinatology, 117997 Moscow, Russia

^* To whom correspondence should be addressed.

Received November 7, 2020; Revised November 11, 2020; Accepted November 11, 2020

---

Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion to the cell; often, these additional targets are glycans. The main receptor for SARS-CoV-2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARS-CoV-2 spike (S) protein with an array of glycoconjugates, including various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lactosamine family. We suggest that parallel influenza infection will promote SARS-CoV-2 adhesion to the respiratory epithelial cells due to the unmasking of lactosamine chains by the influenza virus neuraminidase.

---

KEY WORDS: SARS-CoV-2, spike glycoprotein, glycoconjugates, lactosamine

DOI: 10.1134/S0006297921030019

---