ArticleProceedings of the National Academy of Sciences of the United States of America2014
Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Structural basis for childhood antibody recognition of the human metapneumovirus fusion protein.Nature communications · 2025Article
- Structural Basis for Childhood Antibody Recognition of The Human Metapneumovirus Fusion Protein.bioRxiv : the preprint server for biology · 2025Article
- Covalent Labeling Automated Data Analysis Platform for High Throughput in R (coADAPTr): A Proteome-Wide Data Analysis Platform for Covalent Labeling Experiments.Journal of the American Society for Mass Spectrometry · 2024Article
- A neutralizing antibody prevents postfusion transition of measles virus fusion protein.Science (New York, N.Y.) · 2024Article
- Universal paramyxovirus vaccine design by stabilizing regions involved in structural transformation of the fusion protein.Nature communications · 2024Article
- Structural Studies of Henipavirus Glycoproteins.Viruses · 2024Review
- Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation.Journal of virology · 2023Article
- Structural basis for ultrapotent antibody-mediated neutralization of human metapneumovirus.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- Laser-free Hydroxyl Radical Protein Footprinting to Perform Higher Order Structural Analysis of Proteins.Journal of visualized experiments : JoVE · 2021Article
- Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting.Biochemistry · 2020Article
- Third Helical Domain of the Nipah Virus Fusion Glycoprotein Modulates both Early and Late Steps in the Membrane Fusion Cascade.Journal of virology · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Parainfluenza virus 5 fusion protein maintains pre-fusion stability but not fusogenic activity following mutation of a transmembrane leucine/isoleucine domain.The Journal of general virology · 2020Article
- Fast photochemical oxidation of proteins (FPOP): A powerful mass spectrometry-based structural proteomics tool.The Journal of biological chemistry · 2019Review
- Illuminating Biological Interactions with in Vivo Protein Footprinting.Analytical chemistry · 2019Article
- A Fast Photochemical Oxidation of Proteins (FPOP) platform for free-radical reactions: the carbonate radical anion with peptides and proteins.Free radical biology & medicine · 2019Article
- Fast Photochemical Oxidation of Proteins Coupled with Mass Spectrometry.Protein and peptide letters · 2019Review
- Real Time Normalization of Fast Photochemical Oxidation of Proteins Experiments by Inline Adenine Radical Dosimetry.Analytical chemistry · 2018Article
- Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions.Methods (San Diego, Calif.) · 2018Review
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Authors and funding
10 authors.
Funding
Abstract
To infect a cell, the Paramyxoviridae family of enveloped viruses relies on the coordinated action of a receptor-binding protein (variably HN, H, or G) and a more conserved metastable fusion protein (F) to effect membrane fusion and allow genomic transfer. Upon receptor binding, HN (H or G) triggers F to undergo an extensive refolding event to form a stable postfusion state. Little is known about the intermediate states of the F refolding process. Here, a soluble form of parainfluenza virus 5 F was triggered to refold using temperature and was footprinted along the refolding pathway using fast photochemical oxidation of proteins (FPOP). Localization of the oxidative label to solvent-exposed side chains was determined by high-resolution MS/MS. Globally, metastable prefusion F is oxidized more extensively than postfusion F, indicating that the prefusion state is more exposed to solvent and is more flexible. Among the first peptides to be oxidatively labeled after temperature-induced triggering is the hydrophobic fusion peptide. A comparison of peptide oxidation levels with the values of solvent-accessible surface area calculated from molecular dynamics simulations of available structural data reveals regions of the F protein that lie at the heart of its prefusion metastability. The strong correlation between the regions of F that experience greater-than-expected oxidative labeling and epitopes for neutralizing antibodies suggests that FPOP has a role in guiding the development of targeted therapeutics. Analysis of the residue levels of labeled F intermediates provides detailed insights into the mechanics of this critical refolding event.
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