Effect of Envelope Proteins on the Mechanical Properties of Influenza Virus

Schaap, Iwan A. T.; Eghiaian, Frédéric; Georges, Amédée des; Veigel, Claudia

doi:10.1074/jbc.m112.412726

Cited by 70 publications

(106 citation statements)

References 52 publications

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“…[118][119][120][121][122] Stiffness of the virus can drastically change when the virus is exposed to different environmental conditions, i.e., different pH, ionic strength, etc. An effective multivalent inhibitor must then maximize its binding capacity by possessing a matching array of ligands to the virus surface and increasing its contact area upon binding.…”

Section: Mechanical Properties Of Pathogensmentioning

confidence: 99%

Pathogen Inhibition by Multivalent Ligand Architectures

2016

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Interfacial multivalent interactions at pathogen-cell interfaces can be competitively inhibited by multivalent scaffolds that prevent pathogen adhesion to the cells during the initial stages of infection. The lack of understanding of complex biological systems makes the design of an efficient multivalent inhibitor a toilsome task. Therefore, we have highlighted the main issues and concerns associated with blocking pathogen at interfaces, which are dependent on the nature and properties of both multivalent inhibitors and pathogens, such as viruses and bacteria. The challenges associated with different cores or carrier scaffolds of multivalent inhibitors are concisely discussed with selected examples.

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Section: Mechanical Properties Of Pathogensmentioning

confidence: 99%

Pathogen Inhibition by Multivalent Ligand Architectures

2016

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“…In the case of flat membranes, we discuss the use of diffuse x-ray scattering [43–49], pipette aspiration and tether pulling [50–58], and fluctuation analysis [50,51,59,60]. In the more challenging case of small vesicles, we explore neutron spin echo (NSE) [61–63], and atomic force microscopy (AFM) experiments [64–69]. Finally, we describe the most recent efforts, including our own, to accurately capture bending rigidity from simulations of fluctuating membranes, both in flat bilayers and small vesicles [70–74].…”

Section: Introductionmentioning

confidence: 99%

Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

West

Brummel

Braun

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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We review experimental and simulation approaches that have been used to determine curvature generation and remodeling of lipid bilayers by membrane-bending proteins. Particular emphasis is placed on the complementary approaches used to study α-Synuclein (αSyn), a major protein involved in Parkinson's disease (PD). Recent cellular and biophysical experiments have shown that the protein 1) deforms the native structure of mitochondrial and model membranes; and 2) inhibits vesicular fusion. Today's advanced experimental and computational technology has made it possible to quantify these protein-induced changes in membrane shape and material properties. Collectively, experiments, theory and multi-scale simulation techniques have established the key physical determinants of membrane remodeling and rigidity: protein binding energy, protein partition depth, protein density, and membrane tension. Despite the exciting and significant progress made in recent years in these areas, challenges remain in connecting biophysical insights to the cellular processes that lead to disease. This article is part of a Special Issue entitled: Membrane Proteins edited by J.C. Gumbart and Sergei Noskov.

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“…Schaap et al [63] used simplified model systems such as pure liposomes and reconstituted virosomes made of defined lipids and glycoproteins to address the contribution of the lipid and protein components of the viral envelope while investigating the mechanical stiffness of single native influenza virions. The indentation behavior of native influenza virions appeared biphasic, at first a noisy nonlinear phase of below 100 pN followed by a small drop in the force and then an approximate linear phase starting at~10 nm indentation.…”

Section: Effect Of Envelope On Viral Materials Propertiesmentioning

confidence: 99%

Material Properties of Viral Nanocages Explored by Atomic Force Microscopy

Rosmalen

Roos

Wuite

2014

Methods in Molecular Biology

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Single-particle nanoindentation by atomic force microscopy (AFM) is an emergent technique to characterize the material properties of nano-sized proteinaceous systems. AFM uses a very small tip attached to a cantilever to scan the surface of the substrate. As a result of the sensitive feedback loop of AFM, the force applied by the tip on the substrate during scanning can be controlled and monitored. By accurately controlling this scanning force, topographical maps of fragile substrates can be acquired to study the morphology of the substrate. In addition, mechanical properties of the substrate like stiffness and breaking point can be determined by using the force spectroscopy capability of AFM. Here we discuss basics of AFM operation and how this technique is used to determine the structure and mechanical properties of protein nanocages, in particular viral particles. Knowledge of morphology as well as mechanical properties is essential for understanding viral life cycles, including genome packaging, capsid maturation, and uncoating, but also contributes to the development of diagnostics, vaccines, imaging modalities, and targeted therapeutic devices based on viruslike particles.

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Effect of Envelope Proteins on the Mechanical Properties of Influenza Virus

Cited by 70 publications

References 52 publications

Pathogen Inhibition by Multivalent Ligand Architectures

Pathogen Inhibition by Multivalent Ligand Architectures

Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

Material Properties of Viral Nanocages Explored by Atomic Force Microscopy

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