Analytical Ultracentrifugation Detects Quaternary Rearrangements and Antibody-Induced Conformational Selection of the SARS-CoV-2 Spike Trimer
Analytical ultracentrifugation (AUC) analysis shows that the SARS-CoV-2 trimeric Spike (S) protein adopts different quaternary conformations in solution. The relative abundance of the “open”
and “close” conformations is temperature-dependent, and samples with different storage temperature history have different open/close distributions. Neutralizing antibodies (NAbs) targeting the S
receptor binding domain (RBD) do not alter the conformer populations; by contrast, a NAb targeting a cryptic conformational epitope skews the Spike trimer toward an open conformation. The results highlight AUC, which is typically applied for molecular mass determination of biomolecules as a powerful tool for detecting functionally relevant quaternary protein conformations.
GUERRINI Giuditta;
MĖHN Dóra;
FUMAGALLI Francesco;
GIORIA Sabrina;
PEDOTTI Mattia;
SIMONELLI L.;
BIANCHINI Filippo;
ROBBIANI Davide;
VARANI Luca;
CALZOLAI Luigi;
2023-11-20
MDPI
JRC131342
1422-0067 (online),
https://www.mdpi.com/1422-0067/24/19/14875,
https://publications.jrc.ec.europa.eu/repository/handle/JRC131342,
10.3390/ijms241914875 (online),
Additional supporting files
| File name | Description | File type | |
|---|
