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Crystallographically identical virus capsids display different properties in solution

Nature Structural Biology volume 6, pages 114–116 (1999)Cite this article

Proteolysis and chemical modification experiments were combined with mass spectrometry to investigate viral capsid structural mobility in solution. Protein mass mapping was used to examine protein–RNA interactions and their influence on capsid mobility. Virus–like particles (VLPs) assembled in a baculovirus expression system and containing cellular RNA were compared with authentic virions containing the viral genome. Although the protein capsids were indistinguishable by crystallography, the VLPs were significantly more susceptible to cleavage of coat protein than virions. Results from site directed chemical modification of capsid proteins were also consistent with the proteolysis results. Particles containing cellular RNA were significantly more susceptible to modification. These observations demonstrate that lattice packing forces may mask differences in protein assemblies that are readily detectable in solution and that RNA regulates protein stability in a virus assembly.

The complexity of the viral life cycle, which includes particle assembly, transport to susceptible hosts, host selection and infection, requires that the capsid proteins perform a diverse set of functions with a minimum amount of genetic information. High resolution X–ray analysis of viruses has yielded detailed images of viral capsids in the crystalline state with structural implication for functions such as receptor binding and RNA release. The static nature of these studies requires additional experiments to understand mobility. A very promising recent approach is the use of limited proteolysis combined with peptide mass mapping1,2. It has provided evidence for the dynamic nature of viral capsids and has related capsid mobility to viral infectivity by detecting the exposure of normally internal structures in protease accessible environments

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Figure 1: MALDI–TOF mass spectra of tryptic peptides released from FHV and FHV VLPs.
Figure 2: Mass spectra of amino–acetylation reactions comparing reactivities of v–WT–d vs r–WT–b γ–peptide.

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  1. Departments of Molecular Biology and Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 92037, California, USA

    Brian Bothner, Anette Schneemann, Dawn Marshall, Vijay Reddy, John E. Johnson & Gary Siuzdak

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  1. Brian Bothner
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  2. Anette Schneemann
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  3. Dawn Marshall
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  4. Vijay Reddy
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  6. Gary Siuzdak
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Correspondence to John E. Johnson or Gary Siuzdak.

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Bothner, B., Schneemann, A., Marshall, D. et al. Crystallographically identical virus capsids display different properties in solution. Nat Struct Mol Biol 6, 114–116 (1999). https://doi.org/10.1038/5799

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