Thermodynamic Characterization of Viral Procapsid Expansion into a Functional Capsid Shell

Medina, E; Nakatani, Eri; Kruse, Shannon; Catalano, Carlos Enrique

doi:10.1016/j.jmb.2012.02.020

Cited by 26 publications

(65 citation statements)

References 64 publications

(98 reference statements)

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“…For instance, the expanded structures of HK97 show an increment of the yield force with respect the prohead due to the crosslinking 14 . Our results are compatible with the unique observation that expansion of the lambda procapsid is fully reversible 21 , since the capsid contraction would be more difficult with a stiffer particle. Therefore, we can conclude that the main objective of the expansion, besides increasing the shell volume for DNA accommodation, is the exposure of the hydrophobic patches to provide nucleation sites for gpD trimer spike assembly 21 and not the immediate stabilization.…”

Section: Discussionsupporting

confidence: 90%

“…Our results are compatible with the unique observation that expansion of the lambda procapsid is fully reversible 21 , since the capsid contraction would be more difficult with a stiffer particle. Therefore, we can conclude that the main objective of the expansion, besides increasing the shell volume for DNA accommodation, is the exposure of the hydrophobic patches to provide nucleation sites for gpD trimer spike assembly 21 and not the immediate stabilization. Likewise, our experiments demonstrate that gpD incorporation into the shell induces a major mechanical reinforcement of the capsid in both the stiffness and yield force (Fig.…”

Section: Discussionsupporting

confidence: 90%

“…3e) indicates that the shell loses some strength during expansion. Although thin shell modelling 23 applied to lambda geometry would assign to expanded capsids a Young modulus B5 times larger than procapsids 14 , it is known that the expanded shell is fragile and easily damaged by Transmission electron microscopy (TEM) staining procedures 21 . This finding, together with our results, suggest that the objective of the expansion transition is not the immediate stabilization, as it appears for other phages 30 .…”

Section: Discussionmentioning

confidence: 99%

“…Subsequently, gpD protein adds to hydrophobic patches at the external surface of the expanded shell 21 . While not required for DNA packaging per se, gpD decoration is required to package the full genome length, presumably owing to instability of the shell in its absence.…”

mentioning

confidence: 99%

“…These observations suggest that gpD protein provides the necessary stability to the shell for withstanding the tremendous internal pressure built up during dsDNA packing 22 . In addition, while expanded shells appear fragile under the typical electron microscopy staining preparations, gpD-decorated particles preserve its integrity 21 . These observations have been interpreted to indicate that gpD provides structural stability to the expanded shell, but an objective and systematic demonstration has never been performed on this or any other viral decoration protein.…”

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confidence: 99%

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Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

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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.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Cementing proteins provide extra mechanical stabilization to viral cages

et al. 2014

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Bacteriophage lambda: The path from biology to theranostic agent

Catalano

2018

WIREs Nanomed Nanobiotechnol

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Viral particles provide an attractive platform for the engineering of semisynthetic therapeutic nanoparticles. They can be modified both genetically and chemically in a defined manner to alter their surface characteristics, for targeting specific cell types, to improve their pharmacokinetic features and to attenuate (or enhance) their antigenicity. These advantages derive from a detailed understanding of virus biology, gleaned from decades of fundamental genetic, biochemical, and structural studies that have provided mechanistic insight into virus assembly pathways. In particular, bacteriophages offer significant advantages as nanoparticle platforms and several have been adapted toward the design and engineering of "designer" nanoparticles for therapeutic and diagnostic (theranostic) applications. The present review focuses on one such virus, bacteriophage lambda; I discuss the biology of lambda, the tools developed to faithfully recapitulate the lambda assembly reactions in vitro and the observations that have led to cooptation of the lambda system for nanoparticle design. This discussion illustrates how a fundamental understanding of virus assembly has allowed the rational design and construction of semisynthetic nanoparticles as potential theranostic agents and illustrates the concept of benchtop to bedside translational research. This article is categorized under: Biology-Inspired Nanomaterials> Protein and Virus-Based Structures Biology-Inspired Nanomaterials> Nucleic Acid-Based Structures.

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Atomic Force Microscopy of Protein Shells: Virus Capsids and Beyond

Martín-González

Ortega-Esteban

Moreno‐Madrid

et al. 2017

Single Molecule Analysis

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In Atomic Force Microscopy (AFM) the probe is a nanometric tip located at the end of a microcantilever which palpates the specimen under study as a blind person uses a white cane. In this way AFM allows obtaining nanometric resolution images of individual protein shells, such as viruses, in liquid milieu. Beyond imaging, AFM also enables the manipulation of single protein cages, and the characterization a variety physicochemical properties able of inducing any measurable mechanical perturbation to the microcantilever that holds the tip. In this chapter we start revising some recipes for adsorbing protein shells on surfaces. Then we describe several AFM approaches to study individual protein cages, ranging from imaging to spectroscopic methodologies devoted to extracting physical information, such as mechanical and electrostatic properties.

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Thermodynamic Characterization of Viral Procapsid Expansion into a Functional Capsid Shell

Cited by 26 publications

References 64 publications

Cementing proteins provide extra mechanical stabilization to viral cages

Cementing proteins provide extra mechanical stabilization to viral cages

Bacteriophage lambda: The path from biology to theranostic agent

Atomic Force Microscopy of Protein Shells: Virus Capsids and Beyond

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