Failure of Viral Shells

Klug, William S.; Bruinsma, Robijn; Michel, Jean‐Philippe; Knobler, Charles M.; Ivanovska, Irena L.; Schmidt, Christoph F.; Wuite, Gijs J. L.

doi:10.1103/physrevlett.97.228101

Cited by 143 publications

(133 citation statements)

References 14 publications

Supporting

Mentioning

125

Contrasting

Order By: Relevance

“…It is tempting to assign the force at which the crack is created (yield force) to the elastic limit of the indentation curve (that is, the force value at the first sharp decay after linear indentation). However, the sharp decays of the force can be related to reversible deformations, buckling, slip and rotation of the particle 25,26 . Thus, particles were routinely imaged after the indentation experiment and only those showing evident cracking are considered for statistics.…”

Section: Resultsmentioning

confidence: 99%

Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

View full text Add to dashboard Cite

The study of virus shell stability is key not only for gaining insights into viral biological cycles but also for using viral capsids in materials science. The strength of viral particles depends profoundly on their structural changes occurring during maturation, whose final step often requires the specific binding of 'decoration' proteins (such as gpD in bacteriophage lambda) to the viral shell. Here we characterize the mechanical stability of gpD-free and gpD-decorated bacteriophage lambda capsids. The incorporation of gpD into the lambda shell imparts a major mechanical reinforcement that resists punctual deformations. We further interrogate lambda particle stability with molecular fatigue experiments that resemble the sub-lethal Brownian collisions of virus shells with macromolecules in crowded environments. Decorated particles are especially robust against collisions of a few k B T (where k B is the Boltzmann's constant and T is the temperature B300 K), which approximate those anticipated from molecular insults in the environment.

show abstract

Section: Resultsmentioning

confidence: 99%

Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

View full text Add to dashboard Cite

show abstract

“…1B). Inversioninduced softening of capsids has been observed experimentally and numerically (18,27).…”

Section: [1]mentioning

confidence: 98%

Mechanical limits of viral capsids

Buenemann

Lenz

2007

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We studied the elastic properties and mechanical stability of viral capsids under external force-loading with computer simulations. Our approach allows the implementation of specific geometries corresponding to specific phages, such as 29 and cowpea chlorotic mottle virus. We demonstrate how, in a combined numerical and experimental approach, the elastic parameters can be determined with high precision. The experimentally observed bimodality of elastic spring constants is shown to be of geometrical origin, namely the presence of pentavalent units in the viral shell. We define a criterion for capsid breakage that explains well the experimentally observed rupture. From our numerics we find a crossover from ␥ 2/3 to ␥ 1/2 for the dependence of the rupture force on the Fö ppl-von Ká rmá n number, ␥. For filled capsids, high internal pressures lead to a stronger destabilization for viruses with buckled ground states versus viruses with unbuckled ground states. Finally, we show how our numerically calculated energy maps can be used to extract information about the strength of protein-protein interactions from rupture experiments.biomaterials ͉ membranes ͉ thin shells

show abstract

“…Initially, these theories were applied to the mechanics of thin macroscopic structures, where the relevant elastic constants (a Young's modulus and a bending rigidity) are related to the bulk material properties and the plate or shell thickness. However, these theories have also been successfully applied to describe mechanical properties of microscopic structures, such as viral capsids [8][9][10][11], bacterial cell walls [12][13][14][15], membranes of red blood cells [16][17][18], and hollow polymer and polyelectrolyte capsules [19][20][21][22][23]. Note that in these more microscopic examples, the effective elastic constants are not related to bulk mechanical properties but instead depend on details of microscopic molecular interactions.…”

Section: Introductionmentioning

confidence: 99%

Statistical Mechanics of Thin Spherical Shells

Košmrlj

Nelson

2017

Phys. Rev. X

View full text Add to dashboard Cite

We explore how thermal fluctuations affect the mechanics of thin amorphous spherical shells. In flat membranes with a shear modulus, thermal fluctuations increase the bending rigidity and reduce the inplane elastic moduli in a scale-dependent fashion. This is still true for spherical shells. However, the additional coupling between the shell curvature, the local in-plane stretching modes, and the local out-ofplane undulations leads to novel phenomena. In spherical shells, thermal fluctuations produce a radiusdependent negative effective surface tension, equivalent to applying an inward external pressure. By adapting renormalization group calculations to allow for a spherical background curvature, we show that while small spherical shells are stable, sufficiently large shells are crushed by this thermally generated "pressure." Such shells can be stabilized by an outward osmotic pressure, but the effective shell size grows nonlinearly with increasing outward pressure, with the same universal power-law exponent that characterizes the response of fluctuating flat membranes to a uniform tension.

show abstract

Failure of Viral Shells

Cited by 143 publications

References 14 publications

Cementing proteins provide extra mechanical stabilization to viral cages

Cementing proteins provide extra mechanical stabilization to viral cages

Mechanical limits of viral capsids

Statistical Mechanics of Thin Spherical Shells

Contact Info

Product

Resources

About