Analytical ultracentrifugation detects quaternary rearrangements and antibody-induced conformational selection of the SARS-CoV-2 spike trimer
Informazioni aggiuntive
Autori
Guerrini G.,
Mehn D.,
Fumagalli F.,
Gioria S.,
Pedotti M.,
Simonelli L.,
Bianchini F.,
Robbiani D.,
Varani L.,
Calzolai L.
Tipo
Articolo pubblicato in rivista scientifica
Anno
2023
Lingua
Inglese
Sommario
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.
Parole chiave
SARS-CoV-2, Spike, Trimer, Antibody, AUC, Analytical ultracentrifugation, Sedimentation, Conformation
Periodico
International journal of molecular sciences
Volume
24
Numero ( Mese )
19
Pagine (o numero dell’articolo)
14875
Diffusione
Licenza
CC BY
Visibilità
Pubblico
Status open access
Gold
