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Glycoconj J . SARS-CoV-2 S glycoprotein binding to multiple host receptors enables cell entry and infection

tetano

Editor, Senior Moderator
Glycoconj J


. 2021 Sep 20.
doi: 10.1007/s10719-021-10021-z. Online ahead of print.
SARS-CoV-2 S glycoprotein binding to multiple host receptors enables cell entry and infection


Irena Trbojević-Akmačić[SUP] 1 [/SUP], Tea Petrović[SUP] 2 [/SUP], Gordan Lauc[SUP] 2 3 [/SUP]



Affiliations

Abstract

The severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) infection displays a wide array of clinical manifestations. Although some risk factors for coronavirus disease 2019 (COVID-19) severity and outcomes have been identified the underlying biologic mechanisms are still not well understood. The surface SARS-CoV-2 proteins are heavily glycosylated enabling host cell interaction and viral entry. Angiotensin-converting enzyme 2 (ACE2) has been identified to be the main host cell receptor enabling SARS-CoV-2 cell entry after interaction with its S glycoprotein. However, recent studies report SARS-CoV-2 S glycoprotein interaction with other cell receptors, mainly C-type lectins which recognize specific glycan epitopes facilitating SARS-CoV-2 entry to susceptible cells. Here, we are summarizing the main findings on SARS-CoV-2 interactions with ACE2 and other cell membrane surface receptors and soluble lectins involved in the viral cell entry modulating its infectivity and potentially playing a role in subsequent clinical manifestations of COVID-19.

Keywords: COVID-19; Glycans; Lectins; S glycoprotein; SARS-CoV-2.
 
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