In this report, the interaction between respiratory syncytial virus (RSV) and heat shock protein 70 (HSP70) was examined. Although no significant increase in total HSP70 protein levels was observed during virus infection, analysis of the HSP70 content in lipid-raft membranes from mock- and virus-infected cells revealed an increase in the levels of raft-associated HSP70 during virus infection. Fluorescence microscopy demonstrated that this transport of HSP70 into lipid-raft membranes correlated with the appearance of HSP70 within virus-induced inclusion bodies. Furthermore, co-localisation of HSP70 with the virus N protein and the raft lipid GM1 was observed within these structures. Immunoprecipitation experiments demonstrated the ability of HSP70 to interact with the virus polymerase complex in lipid-rafts in an ATP-dependent manner. Collectively, these data suggest that RSV may induce cellular changes which allow the recruitment of specific host-cell factors, via lipid-raft membranes, to the polymerase complex.
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http://dx.doi.org/10.1016/j.virol.2005.05.004 | DOI Listing |
Langmuir
January 2025
Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110016, India.
Plasma membrane (PM) simulations at longer length and time scales at nearly atomistic resolution can provide invaluable insights into cell signaling, apoptosis, lipid trafficking, and lipid raft formation. We propose a coarse-grained (CG) model of a mammalian PM considering major lipid head groups distributed asymmetrically across the membrane bilayer and validate the model against bilayer structural properties from atomistic simulation. Using the proposed CG model, we identify a recurring pattern in the passive collective cholesterol transbilayer motion and study the individual cholesterol flip-flop events and associated pathways along with lateral ordering in the bilayer during a flip-flop event.
View Article and Find Full Text PDFViruses
November 2024
Department of Biology, Faculty of Medicine, Aix-Marseille University, INSERM UA16, 13015 Marseille, France.
Most studies on the docking of ivermectin on the spike protein of SARS-CoV-2 concern the receptor binding domain (RBD) and, more precisely, the RBD interface recognized by the ACE2 receptor. The N-terminal domain (NTD), which controls the initial attachment of the virus to lipid raft gangliosides, has not received the attention it deserves. In this study, we combined molecular modeling and physicochemical approaches to analyze the mode of interaction of ivermectin with the interface of the NTD-facing lipid rafts of the host cell membrane.
View Article and Find Full Text PDFBiochem Biophys Res Commun
January 2025
Department of Gastroenterology, Juntendo University School of Medicine, Tokyo, Japan.
Lipid rafts are subdomains of the cell membrane that are rich in cholesterol and glycolipids, and they are involved in various cellular processes and pathophysiological mechanisms. However, the specific role of lipid rafts in hepatocyte dysfunction during the pathogenesis of metabolic dysfunction-associated steatotic liver disease (MASLD) is not fully understood. In this study, we investigated the impact of lipid rafts on insulin sensitivity and hepatocyte injury induced by saturated free fatty acids (sFFAs) using primary-cultured mouse hepatocytes.
View Article and Find Full Text PDFMembranes (Basel)
December 2024
Laboratory of Physical-Chemistry, Department of Chemistry, Universidad Nacional del Sur (UNS), Bahía Blanca 8000, Argentina.
The present study investigates a multicomponent lipid system that simulates the neuronal grey matter membrane, employing molecular acoustics as a precise, straightforward, and cost-effective methodology. Given the significance of omega-3 polyunsaturated fatty acids in the functionality of cellular membranes, this research examines the effects of reducing 1-palmitoyl-2-docosahexaenoylphosphatylcholine (PDPC) content on the compressibility and elasticity of the proposed membrane under physiological conditions. Our results align with bibliographic data obtained through other techniques, showing that as the proportion of PDPC increases in the grey matter membrane model, the system's compressibility decreases, and the membrane's elasticity increases, as evidenced by the reduction in the bulk modulus.
View Article and Find Full Text PDFAnal Chem
January 2025
Instituto de Biomedicina y Genética Molecular, Unidad de Excelencia, University of Valladolid-CSIC, Valladolid 47003, Spain.
Lipid rafts are liquid-ordered domains in which specific enzymes and receptors are located. These membrane platforms play crucial roles in a variety of signaling pathways. Alterations in the lipid environment, such as those elicited by oxidative stress, can lead to important functional disruptions in membrane proteins.
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