Analytical ultracentrifugation detects quaternary rearrangements and antibody-induced conformational selection of the SARS-CoV-2 spike trimer
Additional information
Authors
Guerrini G.,
Mehn D.,
Fumagalli F.,
Gioria S.,
Pedotti M.,
Simonelli L.,
Bianchini F.,
Robbiani D.,
Varani L.,
Calzolai L.
Type
Journal Article
Year
2023
Language
English
Abstract
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.
Keywords
SARS-CoV-2, Spike, Trimer, Antibody, AUC, Analytical ultracentrifugation, Sedimentation, Conformation
Journal
International journal of molecular sciences
Volume
24
Number ( Month )
19
Pages (or article number)
14875
Diffusion
License
CC BY
Visibility
Public
Status open access
Gold
