title: Cementing proteins provide extra mechanical stabilization to viral cages.
abstract: 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 kBT (where kB is the Boltzmann's constant and T is the temperature ~300 K), which approximate those anticipated from molecular insults in the environment.
authors: 1] Departamento de Física de la Materia Condensada, Universidad Autónoma de Madrid, 28049 Madrid, Spain [2] Instituto de Física de la Materia Condensada (IFIMAC), Universidad Autónoma de Madrid, 28049 Madrid, Spain.
authors: M
authors: M
authors: Hernando-Pérez
authors: Department of Medicinal Chemistry, School of Pharmacy, University of Washington, H-172 Health Sciences Building, Box 357610, Seattle, Washington 98195. USA.
authors: S
authors: S
authors: Lambert
authors: Department of Medicinal Chemistry, School of Pharmacy, University of Washington, H-172 Health Sciences Building, Box 357610, Seattle, Washington 98195. USA.
authors: E
authors: E
authors: Nakatani-Webster
authors: Department of Medicinal Chemistry, School of Pharmacy, University of Washington, H-172 Health Sciences Building, Box 357610, Seattle, Washington 98195. USA.
authors: C E
authors: CE
authors: Catalano
authors: 1] Departamento de Física de la Materia Condensada, Universidad Autónoma de Madrid, 28049 Madrid, Spain [2] Instituto de Física de la Materia Condensada (IFIMAC), Universidad Autónoma de Madrid, 28049 Madrid, Spain.
authors: P J
authors: PJ
authors: de Pablo
mesh_terms: D010582:Bacteriophage lambda / Q000378:metabolism*; D001696:Biomechanical Phenomena; D001709:Biotechnology / Q000379:methods*; D002213:Capsid / Q000378:metabolism*; D036022:Capsid Proteins / Q000378:metabolism*; D008422:Materials Testing; D018625:Microscopy, Atomic Force
chemical_list: D036022:Capsid Proteins