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Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength.

Publication ,  Journal Article
Michel, JP; Ivanovska, IL; Gibbons, MM; Klug, WS; Knobler, CM; Wuite, GJL; Schmidt, CF
Published in: Proceedings of the National Academy of Sciences of the United States of America
April 2006

The elastic properties of capsids of the cowpea chlorotic mottle virus have been examined at pH 4.8 by nanoindentation measurements with an atomic force microscope. Studies have been carried out on WT capsids, both empty and containing the RNA genome, and on full capsids of a salt-stable mutant and empty capsids of the subE mutant. Full capsids resisted indentation more than empty capsids, but all of the capsids were highly elastic. There was an initial reversible linear regime that persisted up to indentations varying between 20% and 30% of the diameter and applied forces of 0.6-1.0 nN; it was followed by a steep drop in force that is associated with irreversible deformation. A single point mutation in the capsid protein increased the capsid stiffness. The experiments are compared with calculations by finite element analysis of the deformation of a homogeneous elastic thick shell. These calculations capture the features of the reversible indentation region and allow Young's moduli and relative strengths to be estimated for the empty capsids.

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Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

April 2006

Volume

103

Issue

16

Start / End Page

6184 / 6189

Related Subject Headings

  • RNA, Viral
  • Point Mutation
  • Microscopy, Atomic Force
  • Hydrogen-Ion Concentration
  • Genome, Viral
  • Elasticity
  • Capsid Proteins
  • Capsid
  • Bromovirus
 

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Michel, J. P., Ivanovska, I. L., Gibbons, M. M., Klug, W. S., Knobler, C. M., Wuite, G. J. L., & Schmidt, C. F. (2006). Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength. Proceedings of the National Academy of Sciences of the United States of America, 103(16), 6184–6189. https://doi.org/10.1073/pnas.0601744103
Michel, J. P., I. L. Ivanovska, M. M. Gibbons, W. S. Klug, C. M. Knobler, G. J. L. Wuite, and C. F. Schmidt. “Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength.Proceedings of the National Academy of Sciences of the United States of America 103, no. 16 (April 2006): 6184–89. https://doi.org/10.1073/pnas.0601744103.
Michel JP, Ivanovska IL, Gibbons MM, Klug WS, Knobler CM, Wuite GJL, et al. Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength. Proceedings of the National Academy of Sciences of the United States of America. 2006 Apr;103(16):6184–9.
Michel, J. P., et al. “Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength.Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 16, Apr. 2006, pp. 6184–89. Epmc, doi:10.1073/pnas.0601744103.
Michel JP, Ivanovska IL, Gibbons MM, Klug WS, Knobler CM, Wuite GJL, Schmidt CF. Nanoindentation studies of full and empty viral capsids and the effects of capsid protein mutations on elasticity and strength. Proceedings of the National Academy of Sciences of the United States of America. 2006 Apr;103(16):6184–6189.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

April 2006

Volume

103

Issue

16

Start / End Page

6184 / 6189

Related Subject Headings

  • RNA, Viral
  • Point Mutation
  • Microscopy, Atomic Force
  • Hydrogen-Ion Concentration
  • Genome, Viral
  • Elasticity
  • Capsid Proteins
  • Capsid
  • Bromovirus