ArticleRapid communications in mass spectrometry : RCM2010
Determining the topology of virus assembly intermediates using ion mobility spectrometry-mass spectrometry.
Article in Rapid communications in mass spectrometry : RCM, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 86 citations in OpenAlex.
- High-throughput in situ single particle X-ray imaging of dehydrating viral capsids.Light, science & applications · 2026Article
- On the Utility of Infrared Photoactivation for Native Top-Down and Complex-Down Orbitrap Mass Spectrometry of Soluble Proteoform Complexes.Journal of the American Society for Mass Spectrometry · 2026Article
- Roughhousing with Ions: Surface-Induced Dissociation and Electron Capture Dissociation as Diagnostics of Q-Cyclic IMS-TOF Instrument Tuning Gentleness.Journal of the American Society for Mass Spectrometry · 2025Article
- Exploring the Effects of Intersubunit Interface Mutations on Virus-Like Particle Structure and Stability.Biochemistry · 2024Article
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- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Fitness Landscape-Guided Engineering of Locally Supercharged Virus-like Particles with Enhanced Cell Uptake Properties.ACS chemical biology · 2022Article
- Exploring the Conformational and Binding Dynamics of HMGA2·DNA Complexes Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Opening opportunities for KCommunications biology · 2022Article
- Stability and conformational memory of electrosprayed and rehydrated bacteriophage MS2 virus coat proteins.Current research in structural biology · 2022Article
- Subunit pI Can Influence Protein Complex Dissociation Characteristics.Journal of the American Society for Mass Spectrometry · 2019Article
- RNA-Mediated Virus Assembly: Mechanisms and Consequences for Viral Evolution and Therapy.Annual review of biophysics · 2019Review
- Thermodynamic Stability of the Transcription Regulator PaaR2 from Escherichia coli O157:H7.Biophysical journal · 2019Article
- Packaging of Genomic RNA in Positive-Sense Single-Stranded RNA Viruses: A Complex Story.Viruses · 2019Review
- Article
- In-Source Reduction of Disulfide-Bonded Peptides Monitored by Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS.Journal of the American Society for Mass Spectrometry · 2017Article
- Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes.Journal of the American Society for Mass Spectrometry · 2016Article
- ESI-IMS-MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules.Methods (San Diego, Calif.) · 2016Article
- Evidence that avian reovirus σNS is an RNA chaperone: implications for genome segment assortment.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We have combined ion mobility spectrometry-mass spectrometry with tandem mass spectrometry to characterise large, non-covalently bound macromolecular complexes in terms of mass, shape (cross-sectional area) and stability (dissociation) in a single experiment. The results indicate that the quaternary architecture of a complex influences its residual shape following removal of a single subunit by collision-induced dissociation tandem mass spectrometry. Complexes whose subunits are bound to several neighbouring subunits to create a ring-like three-dimensional (3D) architecture undergo significant collapse upon dissociation. In contrast, subunits which have only a single neighbouring subunit within a complex retain much of their original shape upon complex dissociation. Specifically, we have determined the architecture of two transient, on-pathway intermediates observed during in vitro viral capsid assembly. Knowledge of the mass, stoichiometry and cross-sectional area of each viral assembly intermediate allowed us to model a range of potential structures based on the known X-ray structure of the coat protein building blocks. Comparing the cross-sectional areas of these potential architectures before and after dissociation provided tangible evidence for the assignment of the topologies of the complexes, which have been found to encompass both the 3-fold and the 5-fold symmetry axes of the final icosahedral viral shell. Such insights provide unique information about virus assembly pathways that could allow the design of anti-viral therapeutics directed at the assembly step. This methodology can be readily applied to the structural characterisation of many other non-covalently bound macromolecular complexes and their assembly pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.