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Sequestration of membrane cholesterol by cholesterol-binding proteins inhibits SARS-CoV-2 entry into Vero E6 cells
ID Kulma, Magdalena (Author), ID Šakanović, Aleksandra (Author), ID Bedina Zavec, Apolonija (Author), ID Caserman, Simon (Author), ID Omersa, Neža (Author), ID Šolinc, Gašper (Author), ID Orehek, Sara (Author), ID Hafner Bratkovič, Iva (Author), ID Kuhar, Urška (Author), ID Slavec, Brigita (Author), ID Krapež, Uroš (Author), ID Ocepek, Matjaž (Author), ID Kobayashi, Toshihide (Author), ID Kwiatkowska, Katarzyna (Author), ID Jerala, Roman (Author), ID Podobnik, Marjetka (Author), ID Anderluh, Gregor (Author)

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Abstract
Membrane lipids and proteins form dynamic domains crucial for physiological and pathophysiological processes, including viral infection. Many plasma membrane proteins, residing within membrane domains enriched with cholesterol (CHOL) and sphingomyelin (SM), serve as receptors for attachment and entry of viruses into the host cell. Among these, human coronaviruses, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), use proteins associated with membrane domains for initial binding and internalization. We hypothesized that the interaction of lipid-binding proteins with CHOL in plasma membrane could sequestrate lipids and thus affect the efficiency of virus entry into host cells, preventing the initial steps of viral infection. We have prepared CHOL-binding proteins with high affinities for lipids in the plasma membrane of mammalian cells. Binding of the perfringolysin O domain four (D4) and its variant D4$^{E458L}$ to membrane CHOL impaired the internalization of the receptor-binding domain of the SARS-CoV-2 spike protein and the pseudovirus complemented with the SARS-CoV-2 spike protein. SARS-CoV-2 replication in Vero E6 cells was also decreased. Overall, our results demonstrate that the integrity of CHOL-rich membrane domains and the accessibility of CHOL in the membrane play an essential role in SARS-CoV-2 cell entry.

Language:English
Keywords:cholesterol, endocytosis, plasma membrane, membrane domains, pore-forming proteins, SARS-CoV-2, viral infection
Work type:Article
Typology:1.01 - Original Scientific Article
Organization:VF - Veterinary Faculty
Publication status:Published
Publication version:Version of Record
Year:2024
Number of pages:16 str.
Numbering:Vol. 716, art. 149954
PID:20.500.12556/RUL-156325 This link opens in a new window
UDC:577
ISSN on article:1090-2104
DOI:10.1016/j.bbrc.2024.149954 This link opens in a new window
COBISS.SI-ID:194174467 This link opens in a new window
Publication date in RUL:20.05.2024
Views:289
Downloads:49
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Record is a part of a journal

Title:Biochemical and biophysical research communications
Shortened title:Biochem. biophys. res. commun.
Publisher:Elsevier
ISSN:1090-2104
COBISS.SI-ID:18258983 This link opens in a new window

Licences

License:CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.

Secondary language

Language:Slovenian
Keywords:biokemija, SARS-CoV-2, holesterol, endocitoza, beljakovine, koronavirusi

Projects

Funder:ARIS - Slovenian Research and Innovation Agency
Project number:P1-0391
Name:Molekulske interakcije

Funder:ARIS - Slovenian Research and Innovation Agency
Project number:P4-0092
Name:Zdravje živali, okolje in varna hrana

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