Proteomics

Dataset Information

0

Role of the internal disulfide bond in altering the binding properties of SARS-CoV-2 membrane binding peptide to lipid bilayer


ABSTRACT: The SARS-CoV-2 spike protein’s membrane-binding domain bridges the viral and host cell membrane, a critical step in triggering membrane fusion. we investigate how the SARS-CoV-2 spike protein interacts with host cell membranes, focusing on a membrane-binding peptide (MBP) located near the TMPRSS2 cleavage site. We observe that the disulfide bridge stabilizes the MBP’s interaction with the membrane, suggesting a structural role in viral entry.

INSTRUMENT(S):

ORGANISM(S): Coronaviridae Sp.

SUBMITTER: David Alsteens  

LAB HEAD: David Alsteens

PROVIDER: PXD057533 | Pride | 2025-05-07

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
723.MSMS.mgf Mgf
723.mgf Mgf
723_20241105.fasta Fasta
723_Peptides_MSMS_Thermo_20230828.csv Csv
F002424.mzid.gz Mzid
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Publications

Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy.

Zhang Qingrong Q   Rosa Raissa S L RSL   Ray Ankita A   Durlet Kimberley K   Dorrazehi Gol Mohammad GM   Bernardi Rafael C RC   Alsteens David D  

Nature communications 20250102 1


The SARS-CoV-2 spike protein's membrane-binding domain bridges the viral and host cell membrane, a critical step in triggering membrane fusion. Here, we investigate how the SARS-CoV-2 spike protein interacts with host cell membranes, focusing on a membrane-binding peptide (MBP) located near the TMPRSS2 cleavage site. Through in vitro and computational studies, we examine both primed (TMPRSS2-cleaved) and unprimed versions of the MBP, as well as the influence of its conserved disulfide bridge on  ...[more]

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