tetano
Editor, Senior Moderator
ACS Appl Mater Interfaces
. 2023 Jul 6.
doi: 10.1021/acsami.3c03347. Online ahead of print. Physicochemical Nature of SARS-CoV-2 Spike Protein Binding to Human Vimentin
Piotr Deptuła[SUP] 1 [/SUP], Krzysztof Fiedoruk[SUP] 2 [/SUP], Monika Wasilewska[SUP] 3 [/SUP], Łukasz Suprewicz[SUP] 2 [/SUP], Mateusz Cieśluk[SUP] 2 [/SUP], Paulina Żeliszewska[SUP] 3 [/SUP], Magdalena Oćwieja[SUP] 3 [/SUP], Zbigniew Adamczyk[SUP] 3 [/SUP], Katarzyna Pogoda[SUP] 4 [/SUP], Robert Bucki[SUP] 2 [/SUP]
Affiliations
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.
Keywords: SARS-CoV-2; quartz crystal microbalance; single-molecule binding interactions; single-molecule force spectroscopy; vimentin.
. 2023 Jul 6.
doi: 10.1021/acsami.3c03347. Online ahead of print. Physicochemical Nature of SARS-CoV-2 Spike Protein Binding to Human Vimentin
Piotr Deptuła[SUP] 1 [/SUP], Krzysztof Fiedoruk[SUP] 2 [/SUP], Monika Wasilewska[SUP] 3 [/SUP], Łukasz Suprewicz[SUP] 2 [/SUP], Mateusz Cieśluk[SUP] 2 [/SUP], Paulina Żeliszewska[SUP] 3 [/SUP], Magdalena Oćwieja[SUP] 3 [/SUP], Zbigniew Adamczyk[SUP] 3 [/SUP], Katarzyna Pogoda[SUP] 4 [/SUP], Robert Bucki[SUP] 2 [/SUP]
Affiliations
- PMID: 37413693
- DOI: 10.1021/acsami.3c03347
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.
Keywords: SARS-CoV-2; quartz crystal microbalance; single-molecule binding interactions; single-molecule force spectroscopy; vimentin.