The Spike Glycoprotein of SARS-CoV-2 Binds to β1 Integrins Expressed on the Surface of Lung Epithelial Cells

Overview

Journal Viruses

Publisher MDPI

Specialty Microbiology

Date 2021 Apr 30

PMID 33918599

Citations 28

Authors

Eun Jeong Park

Phyoe Kyawe Myint

Michael Gyasi Appiah

Samuel Darkwah

Siqingaowa Caidengbate

Atsushi Ito

Eri Matsuo

Eiji Kawamoto

Arong Gaowa

Motomu Shimaoka

Affiliations

Soon will be listed here.

Abstract

The spike glycoprotein attached to the envelope of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) binds to and exploits angiotensin-converting enzyme 2 (ACE2) as an entry receptor to infect pulmonary epithelial cells. A subset of integrins that recognize the arginyl-glycyl-aspartic acid (RGD) sequence in the cognate ligands has been predicted in silico to bind the spike glycoprotein and, thereby, to be exploited for viral infection. Here, we show experimental evidence that the β1 integrins predominantly expressed on human pulmonary epithelial cell lines and primary mouse alveolar epithelial cells bind to this spike protein. The cellular β1 integrins support adhesive interactions with the spike protein independently of ACE2, suggesting the possibility that the β1 integrins may function as an alternative receptor for SARS-CoV-2, which could be targeted for the prevention of viral infections.

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