Physicochemical Nature of SARS-CoV-2 Spike Protein Binding to Human Vimentin

Overview

Journal ACS Appl Mater Interfaces

Publisher American Chemical Society

Specialties Biomedical Engineering
Biotechnology

Date 2023 Jul 6

PMID 37413693

Authors

Piotr Deptula

Krzysztof Fiedoruk

Monika Wasilewska

Lukasz Suprewicz

Mateusz Ciesluk

Paulina Zeliszewska

Magdalena Ocwieja

Zbigniew Adamczyk

Katarzyna Pogoda

Robert Bucki

Affiliations

Soon will be listed here.

Abstract

Vimentin, a protein that builds part of the cytoskeleton and is involved in many aspects of cellular function, was recently identified as a cell surface attachment site for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The present study investigated the physicochemical nature of the binding between the SARS-CoV-2 S1 glycoprotein receptor binding domain (S1 RBD) and human vimentin using atomic force microscopy and a quartz crystal microbalance. The molecular interactions of S1 RBD and vimentin proteins were quantified using vimentin monolayers attached to the cleaved mica or a gold microbalance sensor as well as in its native extracellular form present on the live cell surface. The presence of specific interactions between vimentin and S1 RBD was also confirmed using in silico studies. This work provides new evidence that cell-surface vimentin (CSV) functions as a site for SARS-CoV-2 virus attachment and is involved in the pathogenesis of Covid-19, providing a potential target for therapeutic countermeasures.

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