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Related Experiment Videos

Mass spectrometry and viral analysis

G Siuzdak1, B Bothner, M Yeager

  • 1Department of Chemistry, The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA.

Chemistry & Biology
|January 1, 1996
PubMed
Summary

Electrospray ionization mass spectrometry can preserve the native structure of large biomolecular complexes like viruses. This technique allows for the analysis of intact viral particles, confirming their structural integrity after ionization.

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Mass Spectrometry

Background:

  • Electrospray ionization (ESI) mass spectrometry is a key technique for analyzing biomolecules.
  • Concerns exist regarding the preservation of native conformation during ESI analysis of biomolecular complexes.
  • Live viruses were utilized to investigate structural integrity during ESI.

Purpose of the Study:

  • To determine if native biomolecular structures are maintained during electrospray ionization mass spectrometry.
  • To assess the utility of ESI for analyzing large supramolecular complexes.

Main Methods:

  • Generation of viral ions using electrospray ionization mass spectrometry.
  • Analysis of filtered viral ions via transmission electron microscopy.

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  • Confirmation of viral viability through plant inoculation.

    • Main Results:

    • Spherical and rod-like viral ultrastructures were retained for rice yellow mottle virus and tobacco mosaic virus, respectively.
    • Transmission electron microscopy confirmed the structural integrity of viral ions post-ESI.
    • Inoculation studies verified the viability of ESI-analyzed tobacco mosaic virus.

    Conclusions:

    • Electrospray ionization is effective for analyzing supramolecular complexes exceeding 40 million Da.
    • Native biomolecular structures are conserved throughout the electrospray ionization process.
    • ESI-MS is a viable method for studying the structure and integrity of large biological assemblies.