Mechanical limits of viral capsids

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 104; no. 24; pp. 9925 - 9930
• Main Authors: Buenemann, Mathias, Lenz, Peter
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 12.06.2007; National Acad Sciences
• Subjects: Bacteriophages; Bending; Capsid; Capsid - chemistry; Computer Simulation; Cowpea chlorotic mottle virus; DNA; Elastic shells; Elasticity; Experiments; Geometry; Internal pressure; Models, Biological; Osmotic Pressure; Physical Sciences; Proteins; Spring constant; Stress, Mechanical; Vertices; Virology; Virus Physiological Phenomena; Viruses; Viruses - chemistry
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.0611472104

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 φ29 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 γ²/³ to γ¹/² for the dependence of the rupture force on the Föppl-von Kármán number, γ. 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.