When cryo-electron tomography uncovers the in cellulo structural organization of the Chikungunya virus replication complex

 

When cryo-electron tomography and sub-tomogram averaging techniques uncover the in cellulo structural organization of the Chikungunya virus replication complex within the plasma membrane

 

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The Chikungunya virus (CHIKV) is a mosquito-borne pathogen responsible for acute musculoskeletal disease in humans. The replication of the viral RNA genome occurs within specialized membranous replication organelles (RO), also known as spherules, which house the viral replication complex. This membranous complex consists of four viral proteins (nsP1-4) along with various cellular partners.

Using a combined approach of cryo-electron tomography on infected human cells at 17 hours post-infection (hpi), sub-tomogram averaging, and cryo-sectioning through CEMOVIS (Cryo-Electron Microscopy of Vitreous Sections), we investigate the structural organization of the replication complex and examine the replication dynamics within the spherules.

Collectively, this study sheds new light on the dynamic behavior of CHIKV replication organelles and the associated viral replication processes at the interface with cell membranes in infected cells.

 

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In situ fate of Chikungunya virus replication organelles

Justine Girard, Olivier Le Bihan, Joséphine Lai-Kee-Him, Maria Girleanu, Eric Bernard, Cedric Castellarin, Matthew Chee, Aymeric Neyret, Danièle Spehner, Xavier Holy, Anne-Laure Favier, Laurence Briant and Patrick Bron

J Virol. 2024 Jun 28:e0036824.doi: 10.1128/jvi.00368-24

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The qbio Master's program [Quantitative Biology: Molecular Mechanisms of Living Systems (parcours IDIL)] at the University of Montpellier is an interdisciplinary curriculum that blends biology, physics, bioinformatics, and quantitative methods to tackle complex biological challenges.
 
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Le Centre de Biologie Structurale (CBS) de Montpellier s’engage à accueillir 6 stagiaires de seconde générale et technologique, du 16 au 27 juin 2025

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Le Centre de Biologie Structurale (CBS) de Montpellier s’engage à accueillir 6 stagiaires de seconde générale et technologique, du 16 au 27 juin 2025.

Durant les 2 semaines passées au laboratoire, les stagiaires répartis en binômes alterneront entre des ateliers de découverte dans différentes disciplines (biologie moléculaire et cellulaire, biochimie, microscopie, biophysique…) et des journées d’observation auprès du personnel exerçant différents métiers de la recherche. A l’issue du stage, les élèves devront réaliser et présenter un poster en lien avec l’une des thématiques scientifiques abordées lors du stage.

Ces stages s’adressent en priorité à des élèves de seconde, s'engageant dans des spécialités scientifiques en première et terminale. Les demandes doivent etre adressées exclusivement via le formulaire:

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En complément, un CV et une lettre de motivation devront être envoyés à l'adresse This email address is being protected from spambots. You need JavaScript enabled to view it. avant le 7 mars 2025 (fichier pdf unique au nom du candidat). Une sélection sera effectuée sur la base de ce dossier. Nous serons aussi particulièrement attentifs à la parité et une liste d’attente sera établie pour pallier tout désistement. Les réponses seront données aux élèves le 14 mars 2025

Il est recommandé de rechercher un autre stage dans l’éventualité où votre candidature ne serait pas retenue.

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Exploring RNA destabilization mechanisms in biomolecular condensates through atomistic simulations

The complex and crowded cellular environment profoundly influences the structural properties and functions of biomolecules, including RNAs. In particular, biomolecular condensates represent an emerging principle for the compartmentalization of RNA and its regulation. Despite their significance, our understanding of their molecular-scale organization and effects on RNA structure remains limited. In this study, we employ atomistic simulations to investigate RNA properties in a crowded peptide environment resembling biomolecular condensates. Our findings reveal that this environment destabilizes RNA secondary structures and promotes extended nonnative conformations. Notably, the composition of peptides—specifically arginine-rich versus lysine-rich—modulates RNA behavior, suggesting that variations in condensate composition can fine-tune RNA activity in health and disease.

 
References: M. Boccalini, Y. Berezovska, G. Bussi, M. Paloni, & A. Barducci, Exploring RNA destabilization mechanisms in biomolecular condensates through atomistic simulations, Proc. Natl. Acad. Sci. U.S.A. 122 (15) e2425261122, https://doi.org/10.1073/pnas.2425261122 (2025).
 
 
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