7 results match your criteria: "Infectious Disease Research Institute of Montpellier (IRIM)[Affiliation]"
Isolation of Viral Biofilms From HTLV-1 Chronically Infected T Cells and Integrity Analysis.
Bio Protoc
December 2024
Infectious Disease Research Institute of Montpellier (IRIM), UMR 9004 CNRS, University of Montpellier, Montpellier, France.
The human T-lymphotropic virus type-1 (HTLV-1) is an oncogenic retrovirus that predominantly spreads through cell-to-cell contact due to the limited infectivity of cell-free viruses. Among various modes of intercellular transmission, HTLV-1 biofilms emerge as adhesive structures, polarized at the cell surface, which encapsulate virions within a protective matrix. This biofilm is supposed to facilitate simultaneous virion delivery during infection.
View Article and Find Full Text PDFBack to the future - 20 years of progress and developments in photonic microscopy and biological imaging.
J Cell Sci
October 2024
Biomedical Imaging Group and Center for Imaging, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
Article Synopsis
- * The group organizes MiFoBio conferences that feature lectures and hands-on workshops, allowing specialists to share insights and reflect on the evolution of microscopy over the years.
- * The 2023 conference included retrospective talks on key topics like multicellular imaging and advancements in imaging technologies, with summaries available on the ImaBio YouTube channel for further learning.
HTLV-1 biofilm polarization maintained by tetraspanin CD82 is required for efficient viral transmission.
mBio
December 2023
Infectious Disease Research Institute of Montpellier (IRIM), UMR CNRS, Montpellier, France.
In the early stages of infection, human T-lymphotropic virus type 1 (HTLV-1) dissemination within its host is believed to rely mostly on cell-to-cell contacts. Past studies unveiled a novel mechanism of HTLV-1 intercellular transmission based on the remodeling of the host-cell extracellular matrix and the generation of cell-surface viral assemblies whose structure, composition, and function resemble bacterial biofilms. These polarized aggregates of infectious virions, identified as viral biofilms, allow the bulk delivery of viruses to target cells and may help to protect virions from immune attacks.
View Article and Find Full Text PDFHuman IRF1 governs macrophagic IFN-γ immunity to mycobacteria.
Cell
February 2023
Laboratory of Human Genetics of Infectious Diseases, Inserm U1163, 75015 Paris, France; Paris Cité University, Imagine Institute, 75015 Paris, France; St. Giles Laboratory of Human Genetics of Infectious Diseases, The Rockefeller University, New York, NY 10065, USA; Study Center for Primary Immunodeficiencies, Necker Hospital for Sick Children, AP-HP, 75015 Paris, France. Electronic address:
Article Synopsis
- Inborn errors affecting the immune response to IFN-γ lead to mycobacterial diseases, while errors in IFN-α/β impact defense against viral infections.
- A study of children with complete IRF1 deficiency showed they suffered from severe mycobacterial infections but displayed normal responses to various viruses, including SARS-CoV-2.
- IRF1 plays a crucial role in the immune response to mycobacteria, enhancing IFN-γ responses, while its absence does not significantly hinder antiviral defenses associated with IFN-α/β.
Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53.
Elife
June 2021
Infectious disease Research Institute of Montpellier (IRIM), CNRS UMR 9004, University of Montpellier, Montpellier, France.
Article Synopsis
- The study demonstrates that the I-BAR protein IRSp53 is essential for HIV-1 particle formation by aiding the necessary membrane curvature alongside the Gag protein.
- When IRSp53 is knocked down using siRNA, there’s a notable reduction in the production of viral particles, leading to incomplete assembly during the budding process.
- The research highlights a direct interaction between IRSp53 and Gag at the plasma membrane, suggesting that IRSp53 not only supports membrane curvature but is also found in the structure of the HIV-1 particles.
Author Correction: Single molecule localisation microscopy reveals how HIV-1 Gag proteins sense membrane virus assembly sites in living host CD4 T cells.
Sci Rep
November 2018
Infectious Disease Research Institute of Montpellier (IRIM), UMR9004 CNRS, University of Montpellier, 1919 route de Mende, 34293, Montpellier, France.
A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper.
View Article and Find Full Text PDFSingle molecule localisation microscopy reveals how HIV-1 Gag proteins sense membrane virus assembly sites in living host CD4 T cells.
Sci Rep
November 2018
Infectious Disease Research Institute of Montpellier (IRIM), UMR9004 CNRS, University of Montpellier, 1919 route de Mende, 34293, Montpellier, France.
Monitoring virus assembly at the nanoscale in host cells remains a major challenge. Human immunodeficiency virus type 1 (HIV-1) components are addressed to the plasma membrane where they assemble to form spherical particles of 100 nm in diameter. Interestingly, HIV-1 Gag protein expression alone is sufficient to produce virus-like particles (VLPs) that resemble the immature virus.
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