Epitope Mapping of Japanese Encephalitis Virus Neutralizing Antibodies by Native Mass Spectrometry and Hydrogen/Deuterium Exchange.

antibody/antigen interactions epitope mapping hydrogen/deuterium exchange monoclonal antibodies native MS

Journal

Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414

Informations de publication

Date de publication:
20 Mar 2024
Historique:
received: 26 02 2024
revised: 12 03 2024
accepted: 14 03 2024
medline: 28 3 2024
pubmed: 28 3 2024
entrez: 28 3 2024
Statut: epublish

Résumé

Japanese encephalitis virus (JEV) remains a global public health concern due to its epidemiological distribution and the existence of multiple strains. Neutralizing antibodies against this infection have shown efficacy in in vivo studies. Thus, elucidation of the epitopes of neutralizing antibodies can aid in the design and development of effective vaccines against different strains of JEV. Here, we describe a combination of native mass spectrometry (native-MS) and hydrogen/deuterium exchange mass spectrometry (HDX-MS) to complete screening of eight mouse monoclonal antibodies (MAbs) against JEV E-DIII to identify epitope regions. Native-MS was used as a first pass to identify the antibodies that formed a complex with the target antigen, and it revealed that seven of the eight monoclonal antibodies underwent binding. Native mass spectra of a MAb (JEV-27) known to be non-binding showed broad native-MS peaks and poor signal, suggesting the protein is a mixture or that there are impurities in the sample. We followed native-MS with HDX-MS to locate the binding sites for several of the complex-forming antibodies. This combination of two mass spectrometry-based approaches should be generally applicable and particularly suitable for screening of antigen-antibody and other protein-protein interactions when other traditional approaches give unclear results or are difficult, unavailable, or need to be validated.

Identifiants

pubmed: 38540792
pii: biom14030374
doi: 10.3390/biom14030374
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIH HHS
ID : R01 AI073755
Pays : United States
Organisme : NIH HHS
ID : 75N93019C00062
Pays : United States
Organisme : NIH HHS
ID : 75N93022C00035
Pays : United States
Organisme : NIH HHS
ID : P41GM103422
Pays : United States
Organisme : NIH HHS
ID : R24GM136766
Pays : United States

Auteurs

Jagat Adhikari (J)

Department of Chemistry, Washington University in St. Louis, Saint Louis, MO 63130, USA.

James Heffernan (J)

Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63130, USA.

Melissa Edeling (M)

Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63130, USA.

Estefania Fernandez (E)

Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63130, USA.

Prashant N Jethva (PN)

Department of Chemistry, Washington University in St. Louis, Saint Louis, MO 63130, USA.

Michael S Diamond (MS)

Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63130, USA.
Department of Medicine, Washington University School of Medicine, Saint Louis, MO 63130, USA.
Andrew M. and Jane M. Bursky Center for Human Immunology and Immunotherapy Programs, Washington University School of Medicine, Saint Louis, MO 63130, USA.
Department of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO 63130, USA.

Daved H Fremont (DH)

Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63130, USA.
Department of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO 63130, USA.
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63130, USA.

Michael L Gross (ML)

Department of Chemistry, Washington University in St. Louis, Saint Louis, MO 63130, USA.

Classifications MeSH