Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Coronaviridae Sp.
SUBMITTER:
David Alsteens
LAB HEAD: David Alsteens
PROVIDER: PXD057533 | Pride | 2025-05-07
REPOSITORIES: Pride
| 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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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]