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Biomolecules
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The Illumination of Biophysical Mechanisms by Hydrogen Exchange: A Themed...
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The Illumination of Biophysical Mechanisms by Hydrogen Exchange: A Themed Issue in Honor of Professor S. Walter Englander

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: 31 August 2024 | Viewed by 1574

Special Issue Editor

Prof. Dr. A. Joshua Wand

E-Mail Website
Guest Editor
Department of Biochemistry & Biophysics, Texas A&M University, College Station, TX 77845, USA
Interests: protein biophysics; protein thermodynamics; protein dynamics; allostery; protein design & engineering; NMR spectroscopy

Special Issue Information

Dear Colleagues,

I am pleased to announce that Biomolecules will dedicate a Special Issue in honor of Professor Walter Englander in recognition of his seminal contributions to the development of the phenomenon of hydrogen exchange as a tool to investigate protein thermodynamics, dynamics, and function. Entitled “The illumination of biophysical mechanisms by hydrogen exchange,” this themed issue is intended to highlight the powerful capabilities of hydrogen exchange (HX) to reveal fundamental properties of proteins ranging from their stability, folding, dynamics, and function. Contributions are invited that focus on advancing or utilizing hydrogen exchange (HX) techniques in addressing inquiries about biomolecular structure, dynamics, and function. This call for submissions is specifically directed towards the protein biochemistry and biophysics communities. Contributions will be reviewed as usual; publication charges will apply. We ask that you provide your manuscript for review by the end of August 2024.

Prof. Dr. A. Joshua Wand
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • hydrogen exchange chemistry
  • HX–NMR
  • HX-MS
  • protein folding
  • allostery
  • protein binding
  • protein thermodynamics
  • protein biophysics
  • protein function

Published Papers (1 paper)

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Research

14 pages, 2983 KiB  
Article
Epitope Mapping of Japanese Encephalitis Virus Neutralizing Antibodies by Native Mass Spectrometry and Hydrogen/Deuterium Exchange
by Jagat Adhikari, James Heffernan, Melissa Edeling, Estefania Fernandez, Prashant N. Jethva, Michael S. Diamond, Daved H. Fremont and Michael L. Gross
Biomolecules 2024, 14(3), 374; https://doi.org/10.3390/biom14030374 - 20 Mar 2024
Viewed by 1383
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue The Illumination of Biophysical Mechanisms by Hydrogen Exchange: A Themed Issue in Honor of Professor S. Walter Englander)
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