Frank Gondelaud

ORCID: 0000-0003-0061-2405
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About
Contact & Profiles
Research Areas
  • Virology and Viral Diseases
  • Viral Infections and Vectors
  • Protein Structure and Dynamics
  • Proteoglycans and glycosaminoglycans research
  • HIV Research and Treatment
  • Enzyme Structure and Function
  • Glycosylation and Glycoproteins Research
  • interferon and immune responses
  • Mosquito-borne diseases and control
  • vaccines and immunoinformatics approaches
  • Cell Adhesion Molecules Research
  • Vector-Borne Animal Diseases
  • Erythrocyte Function and Pathophysiology
  • Blood properties and coagulation
  • Plant Virus Research Studies
  • Microbial Metabolic Engineering and Bioproduction
  • Prion Diseases and Protein Misfolding
  • Advanced Proteomics Techniques and Applications
  • Advanced Electron Microscopy Techniques and Applications
  • RNA Research and Splicing
  • Bioinformatics and Genomic Networks
  • Mass Spectrometry Techniques and Applications
  • Microtubule and mitosis dynamics
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Hemoglobinopathies and Related Disorders

Architecture et Fonction des Macromolécules Biologiques
2021-2025

Centre National de la Recherche Scientifique
2016-2025

Aix-Marseille Université
2021-2025

Université Claude Bernard Lyon 1
2016-2020

Institut de Chimie et Biochimie Moléculaires et Supramoléculaires
2016-2020

Institut National des Sciences Appliquées de Lyon
2020

Abstract Hendra virus (HeV) is a biosafety level 4 human pathogen belonging to the Henipavirus genus within Paramyxoviridae family. In HeV, phosphoprotein‐encoding gene also drives synthesis of V and W proteins that are two major players in host innate immune response evasion. These three share common intrinsically disordered N‐terminal domain (NTD) have distinct C‐terminal domains. We recently reported ability short region (i.e., PNT3), located shared NTD, form fibrils. subsequently...

10.1002/pro.70068 article EN cc-by-nc Protein Science 2025-02-22

Abstract The Protein Ensemble Database (PED) (URL: https://proteinensemble.org) is the primary resource for depositing structural ensembles of intrinsically disordered proteins. This updated version PED reflects advancements in field, denoting a continual expansion with total 461 entries and 538 ensembles, including those generated without explicit experimental data through novel machine learning (ML) techniques. With this significant increment number few yet-unprecedented new entered...

10.1093/nar/gkad947 article EN cc-by Nucleic Acids Research 2023-10-30

Henipaviruses are BSL-4 zoonotic pathogens responsible in humans for severe encephalitis. Their V protein is a key player the evasion of host innate immune response. We previously showed that Henipavirus proteins consist long intrinsically disordered N-terminal domain (NTD) and β-enriched C-terminal (CTD). These terminals critical binding to DDB1, which cellular component ubiquitin ligase E3 complex, as well MDA5 LGP2, two sensors viral RNA. Here, we serendipitously discovered Hendra virus...

10.3390/biom11091324 article EN cc-by Biomolecules 2021-09-07

The Hendra (HeV) and Nipah (NiV) viruses are high-priority, biosafety level-4 pathogens that cause fatal neurological respiratory disease. Their P gene encodes not only the protein, an essential polymerase cofactor, but also virulence factors V W. We previously showed W protein of HeV (WHeV) forms amyloid-like fibrils one its subdomains, PNT3, fibrillates in isolation. However, fibrillation kinetics is much faster case full-length WHeV compared to suggesting another region contributes...

10.1002/pro.70085 article EN cc-by-nc-nd Protein Science 2025-03-18

Abstract The Hendra and Nipah viruses (HeV NiV) are zoonotic biosafety level-4 pathogens within the Paramyxoviridae family. We previously showed that their W proteins form amyloid-like fibrils in vitro . Here, we demonstrate also forms cellula cysteine residues crucial dictating ability of to fibrillate. oxidation state acts as a switch generate either amorphous aggregates or flexible fibrils. Ectopic expression HeV induces an oxidative stress were observed nuclei different cell lines, with...

10.1101/2024.01.22.576663 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-01-23

The Nipah and Hendra viruses are severe human pathogens. In addition to the P protein, their gene also encodes V W proteins that share with N‐terminal intrinsically disordered domain (NTD) possess distinct C‐terminal domains (CTDs). protein is a key player in evasion of host innate immune response. We previously showed can form amyloid‐like fibrils. However, structural information on CTD (CTD ) its potential contribution fibrillation process lacking. this study, we demonstrate WS able dimers...

10.1111/febs.17239 article EN cc-by-nc FEBS Journal 2024-08-23

Henipaviruses are severe human pathogens within the Paramyxoviridae family. Beyond P protein, Henipavirus gene also encodes V and W proteins which share with their N-terminal, intrinsically disordered domain (NTD) possess a unique C-terminal domain. antagonize interferon (IFN) signaling through NTD-mediated binding to STAT1 STAT4, prevent type I IFN expression production of chemokines. Structural molecular information on is lacking. By combining various bioinformatic approaches, we herein...

10.3390/ijms23020923 article EN International Journal of Molecular Sciences 2022-01-15

The Nipah and Hendra viruses (NiV HeV) are biosafety level 4 human pathogens classified within the Henipavirus genus of Paramyxoviridae family. In both NiV HeV, gene encoding Phosphoprotein (P protein), an essential polymerase cofactor, also encodes V W proteins. These three proteins, which share intrinsically disordered N-terminal domain (NTD) have unique C-terminal domains (CTD), all known to counteract host innate immune response, with acting by either counteracting or inhibiting...

10.3390/ijms24010399 article EN International Journal of Molecular Sciences 2022-12-26

Syndecans are membrane proteoglycans regulating extracellular matrix assembly, cell adhesion and signaling. Their ectodomains can be shed from the surface, act as paracrine autocrine effectors or competitors of full-length syndecans. We report first biophysical characterization recombinant four human syndecans using techniques, show that they behave like flexible random-coil intrinsically disordered proteins, adopt several conformation ensembles in solution. have characterized their...

10.1016/j.mbplus.2021.100081 article EN cc-by-nc-nd Matrix Biology Plus 2021-07-19

Abstract The Nipah and Hendra viruses (NiV HeV ) are biosafety level 4 human pathogens classified within the Henipavirus genus of Paramyxoviridae family. In both NiV HeV, gene encoding Phosphoprotein (P protein), an essential polymerase cofactor, also encodes V W proteins. These three proteins, which share intrinsically disordered N-terminal domain (NTD) have unique C-terminal domains (CTD), all known to counteract host innate immune response, with acting by either counteracting or...

10.1101/2022.11.02.514851 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-11-02
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