Publications associées à Capside

Microsecond time-resolved cryo-electron microscopy

Microsecond time-resolved cryo-electron microscopy has emerged as a novel approach for directly observing protein dynamics. By providing microsecond temporal and near-atomic spatial resolution, it has the potential to elucidate a wide range of dynamics tha ...

2024

Influence of Amino Acid Substitutions in Capsid Proteins of Coxsackievirus B5 on Free Chlorine and Thermal Inactivation

Tamar Kohn, Aleksandar Antanasijevic, Shotaro Torii, Kiruthika Kumar

The sensitivity of enteroviruses to disinfectants varies among genetically similar variants and coincides with amino acid changes in capsid proteins, although the effect of individual substitutions remains unknown. Here, we employed reverse genetics to inv ...

2024

Stimulus-responsive assembly of nonviral nucleocapsids

Angela Steinauer

Controlled assembly of a protein shell around a viral genome is a key step in the life cycle of many viruses. Here we report a strategy for regulating the co-assembly of nonviral proteins and nucleic acids into highly ordered nucleocapsids in vitro. By fus ...

Nature Portfolio2024

Simultaneous membrane and RNA binding by Tick-Borne Encephalitis Virus capsid protein

Sarah Victoria Barrass

Tick-borne encephalitis virus is an enveloped, pathogenic, RNA virus in the family Flaviviridae, genus Flavivirus. Viral particles are formed when the nucleocapsid, consisting of an RNA genome and multiple copies of the capsid protein, buds through the end ...

PUBLIC LIBRARY SCIENCE2023

Susceptibility of enveloped and non-enveloped viruses to ultraviolet light-emitting diode (UV-LED) irradiation and implications for virus inactivation mechanisms

Shotaro Torii

Ultraviolet (UV) light-emitting diodes (UV-LEDs), a disinfection technology, efficiently inactivate pathogens in water. However, the assessment of UV-LED treatment and the mechanisms of UV inactivation on viruses (especially enveloped viruses) are limited. ...

ROYAL SOC CHEMISTRY2023

Genotype-Dependent Kinetics of Enterovirus Inactivation by Free Chlorine and Ultraviolet (UV) Irradiation

Tamar Kohn, Shotaro Torii

Inactivation kinetics of enterovirus by disinfection is often studied using a single laboratory strain of a given genotype. Environmental variants of enterovirus are genetically distinct from the corresponding laboratory strain, yet it is poorly understood ...

2022

Salt enhances the thermostability of enteroviruses by stabilizing capsid protein interfaces

Tamar Kohn, Matteo Dal Peraro, Simon Meister, Alessio Prunotto

Enteroviruses are common agents of infectious disease that are spread by the fecal-oral route. They are readily inactivated by mild heat, which causes the viral capsid to disintegrate or undergo conformational change. While beneficial for the thermal treat ...

American Society for Microbiology2020

Control of Waterborne Human Viruses by Indigenous Bacteria and Protists Is Influenced by Temperature, Virus Type, and Microbial Species

Tamar Kohn, Margot Ninon Lauren Olive, Anna Carratala Ripolles

Human viruses are ubiquitous contaminants in surface waters, where they can persist over extended periods of time. Among the factors governing their environmental persistence, the control (removal or inactivation) by microorganisms remains poorly understoo ...

2020

Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies

David Lyndon Emsley, Marc Anthony Caporini

We report dynamic nuclear polarization (DNP)-enhanced magic-angle spinning (MAS) NMR spectroscopy in viral capsids from HIV-1 and bacteriophage AP205. Viruses regulate their life cycles and infectivity through modulation of their structures and dynamics. W ...

2019

High-speed photothermal off-resonance atomic force microscopy reveals assembly routes of centriolar scaffold protein SAS-6

Pierre Gönczy, Adrian Pascal Nievergelt, Georg Fantner, Niccolo Banterle, Santiago Harald Andany

The self-assembly of protein complexes is at the core of many fundamental biological processes1, ranging from the polymerization of cytoskeletal elements, such as microtubules2, to viral capsid formation and organelle assembly3. To reach a comprehensive un ...

2018