Integrin activation is an essential component of SARS-CoV-2 infection.

ABSTRACT: SARS-CoV-2 infection depends on binding its spike (S) protein to angiotensin-converting enzyme 2 (ACE2). The S protein expresses an RGD motif, suggesting that integrins may be co-receptors. Here, we UV-inactivated SARS-CoV-2 and fluorescently labeled the envelope membrane with octadecyl rhodamine B (R18) to explore the role of integrin activation in mediating cell entry and productive infection. We used flow cytometry and confocal microscopy to show that SARS-CoV-2^R18 particles engage basal-state integrins. Furthermore, we demonstrate that Mn²⁺, which induces integrin extension, enhances cell entry of SARS-CoV-2^R18. We also show that one class of integrin antagonist, which binds to the αI MIDAS site and stabilizes the inactive, closed conformation, selectiv

SUBMITTER: Simons P 

PROVIDER: S-EPMC8516859 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature