A5023384247- Lipid Membrane Structure and Behavior
- Viral Infections and Immunology Research
- Cell Adhesion Molecules Research
- RNA Interference and Gene Delivery
- Cytomegalovirus and herpesvirus research
- RNA Research and Splicing
- HIV Research and Treatment
- Plant Virus Research Studies
- Monoclonal and Polyclonal Antibodies Research
- RNA and protein synthesis mechanisms
- RNA modifications and cancer
- Autophagy in Disease and Therapy
- Force Microscopy Techniques and Applications
- Cellular transport and secretion
- Influenza Virus Research Studies
- Mosquito-borne diseases and control
- Bacteriophages and microbial interactions
- Venomous Animal Envenomation and Studies
- Viral Infections and Vectors
- Viral gastroenteritis research and epidemiology
Umeå University
2021-2024
Centre de Biologie Structurale
2014-2019
Inserm
2014-2019
Université de Montpellier
2014-2019
Centre National de la Recherche Scientifique
2014-2019
Institute of Environmental Biology and Biotechnology
2014
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2014
Abstract Enteroviruses are non-enveloped positive-sense RNA viruses that cause diverse diseases in humans. Their rapid multiplication depends on remodeling of cytoplasmic membranes for viral genome replication. It is unknown how virions assemble around these newly synthesized genomes and they then loaded into autophagic release through secretory autophagy. Here, we use cryo-electron tomography infected cells to show poliovirus assembles directly replication membranes. Pharmacological...
Membrane partition and remodeling play a key role in numerous cell mechanisms, especially viral replication cycles where viruses subvert the plasma membrane to enter escape from host cell. Specifically assembly release of HIV-1 particles require specific cellular components, which are recruited egress site by protein Gag. We previously demonstrated that alters both partitioning dynamics tetraspanins CD9 CD81, players many infectious processes, forming enriched areas virus buds. In this study...
Summary Protein conformational variability (or dynamics) for large macromolecules and its implication their biological function attracts more attention. Collective motions of domains increase the ability a protein to bind partner molecules. Using atomic force microscopy (AFM) topographic images, it is possible take snapshots multi-component at single molecule level reconstruct complete molecular conformations. Here, we report application reconstruction protocol, named AFM-assembly,...
Abstract Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes. ATG2A and ATG9A play an essential role in autophagy mediating lipid transfer re-equilibration between membranes for autophagosome formation. Here we report cryo-EM structures human ATG2A-WIPI4 complex at 3.2 Å, ATG2A-WIPI4-ATG9A 7 Å resolution. The structure a central hydrophobic cavity formed network β-strands that facilitates transfer, highly flexible N- C-terminal domains. Molecular...
Viruses are masters at using cellular pathways to aid their replication. Cryo-electron tomography of poliovirus-infected cells revealed how it utilizes macroautophagy its advantage. Assembly these non-enveloped virions takes place directly on membranes and requires PIK3C3/VPS34 activity be completed, whereas the canonical autophagy inducer ULK1 restricts virus assembly. The tomograms further that enterovirus-induced is selective for RNA-loaded virions, which may help ensure maximum...
Enteroviruses are a vast genus of positive-sense RNA viruses that cause diseases ranging from common cold to poliomyelitis and viral myocarditis. They encode membrane-bound AAA+ ATPase, 2C, has been suggested serve several roles in virus replication, e.g. as an helicase capsid assembly factor. Here, we report the reconstitution full-length, poliovirus 2C's association with membranes. We show N-terminal membrane-binding domain 2C contains conserved glycine, which is by structure predictions...
Influenza virus infection is a serious public health problem in the world, and understanding molecular mechanisms involved viral replication crucial. In this paper, we used minimalist approach based on lipid bilayer supported mica, which imaged by atomic force microscopy (AFM) physiological buffer, to analyze different steps of influenza fusion, from interaction intact viruses with their complete fusion. Our results show that sialic acid recognition priming upon acidification are sufficient...
Flaviviruses replicate their genomes in replication organelles (ROs) formed as bud-like invaginations on the endoplasmic reticulum (ER) membrane, which also functions site for virion assembly. While this localization is well established, it not known to what extent viral membrane remodeling, genome replication, assembly, and maturation are coordinated. Here, we imaged tick-borne flavivirus human cells using cryo-electron tomography. We find that RO bud shaped by a combination of...
SUMMARY HIV-1 assembly specifically alters both partitioning and dynamics of the tetraspanins CD9 CD81 forming enriched areas where virus buds. Importantly presence these proteins at exit sites in viral particles inhibits virus-induced membrane fusion. To get molecular insights into this context, we correlated nanoscale mapping obtained by super resolution microscopy to topography probed Atomic Force Microscopy (AFM). We demonstrated that is trapped within nascent particles, especially buds...
Abstract Enteroviruses are non-enveloped positive-sense RNA viruses that cause diverse diseases in humans. Their rapid multiplication depends on remodeling of cytoplasmic membranes for viral genome replication. It is unknown how virions assemble around these newly synthesized genomes and they then loaded into autophagic release through secretory autophagy. Here, we use cryo-electron tomography infected cells to show poliovirus assembles directly replication membranes. Pharmacological...
Abstract Enteroviruses are a vast genus of positive-sense RNA viruses that cause diseases ranging from common cold to poliomyelitis and viral myocarditis. They encode membrane-bound AAA+ ATPase, 2C, has been suggested serve several roles in virus replication, e.g. as an helicase capsid assembly factor. Here, we report the reconstitution full-length, poliovirus 2C’s association with membranes. We show N-terminal membrane-binding domain 2C contains conserved glycine, which is by structure...