Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells

Author:

Amraei Razie1,Xia Chaoshuang2ORCID,Olejnik Judith34ORCID,White Mitchell R.34ORCID,Napoleon Marc A.5,Lotfollahzadeh Saran5ORCID,Hauser Blake M.67,Schmidt Aaron G.67ORCID,Chitalia Vipul589,Mühlberger Elke34ORCID,Costello Catherine E.2ORCID,Rahimi Nader1ORCID

Affiliation:

1. Department of Pathology, Boston University School of Medicine, Boston, MA 02118

2. Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA 02118

3. Department of Microbiology, Boston University School of Medicine, Boston, MA 02118

4. National Emerging Infectious Diseases Laboratories, Boston University, Boston, MA 02118

5. Renal Section, Department of Medicine, Boston University Medical Center, Boston, MA 02118

6. Ragon Institute of Massachusetts General Hospital (MGH), Massachusetts Institute of Technology and Harvard University, Cambridge, MA 02139

7. Department of Microbiology, Harvard Medical School, Boston, MA 02115

8. Veterans Affairs Boston Healthcare System, Boston, MA 02118

9. Institute of Medical Engineering and Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139

Abstract

Significance Human angiotensin-converting enzyme 2 (ACE2) is the most widely known entry receptor for SARS-CoV-2. The possible involvement of other cellular components in viral entry mechanisms remains unknown. Vimentin is expressed in human endothelial cells, binds to SARS-CoV-2-spike, and expedites SARS-CoV-2 entry. Treatment of lung ACE2/A549 carcinoma cells with purified vimentin or coculture of ACE2/A549 cells with HEK-293 cells expressing vimentin increased ACE2-dependent viral entry. CR3022 antibody blocked vimentin interaction with SARS-CoV-2-spike and inhibited SARS-CoV-2 entry. Vimentin could facilitate SARS-CoV-2 infection and contribute to vascular complications associated with COVID-19.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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