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SARS-CoV-2 S glycoprotein binding to multiple host receptors enables cell entry and infection (CROSBI ID 299187)

Prilog u časopisu | pregledni rad (stručni) | međunarodna recenzija

Trbojević-Akmačić, Irena ; Petrović, Tea ; Lauc, Gordan SARS-CoV-2 S glycoprotein binding to multiple host receptors enables cell entry and infection // Glycoconjugate journal, 38 (2021), 5; 611-623. doi: 10.1007/s10719-021-10021-z

Podaci o odgovornosti

Trbojević-Akmačić, Irena ; Petrović, Tea ; Lauc, Gordan

engleski

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

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.

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

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Podaci o izdanju

38 (5)

2021.

611-623

objavljeno

0282-0080

1573-4986

10.1007/s10719-021-10021-z

Povezanost rada

Biologija, Interdisciplinarne prirodne znanosti, Kliničke medicinske znanosti

Poveznice
Indeksiranost