Analytical ultracentrifugation detects quaternary rearrangements and antibody-induced conformational selection of the SARS-CoV-2 spike trimer
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Guerrini, Giuditta
European Commission, Joint Research Centre (JRC), Ispra, Italy
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Mehn, Dora
European Commission, Joint Research Centre (JRC), Ispra, Italy
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Fumagalli, Francesco
European Commission, Joint Research Centre (JRC), Ispra, Italy
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Gioria, Sabrina
European Commission, Joint Research Centre (JRC), Ispra, Italy
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Pedotti, Mattia
ORCID
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Simonelli, Luca
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Bianchini, Filippo
ORCID
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Robbiani, Davide F.
ORCID
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Varani, Luca
ORCID
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Calzolai, Luigi
European Commission, Joint Research Centre (JRC), Ispra, Italy
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Published in:
- International journal of molecular sciences. - 2023, vol. 24, no. 19, p. 14875
English
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.
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Medicine
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CC BY
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gold
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https://n2t.net/ark:/12658/srd1332081
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