ArticleJournal of virology2008
Overexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion protein.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- A novel luciferase-based assay for quantifying coronavirus-induced syncytia.Scientific reports · 2025Article
- Erp57 facilitates ZIKV-induced DNA damage via NS2B/NS3 complex formation.Emerging microbes & infections · 2024Article
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- Cysteines and N-Glycosylation Sites Conserved among All Alphaherpesviruses Regulate Membrane Fusion in Herpes Simplex Virus 1 Infection.Journal of virology · 2017Article
- Decoding protein networks during virus entry by quantitative proteomics.Virus research · 2016Review
- Inflammatory and oxidative stress in rotavirus infection.World journal of virology · 2016Review
- Murine immune responses to virus-like particle-associated pre- and postfusion forms of the respiratory syncytial virus F protein.Journal of virology · 2015Article
- Review
- Modification of the respiratory syncytial virus f protein in virus-like particles impacts generation of B cell memory.Journal of virology · 2014Article
- PROTEIN DISULFIDE ISOMERASE LIKE 5-1 is a susceptibility factor to plant viruses.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.European journal of immunology · 2013Review
- The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Journal of virology · 2011Article
- Protein disulfide isomerase and host-pathogen interaction.TheScientificWorldJournal · 2011Review
- Assembly and immunological properties of Newcastle disease virus-like particles containing the respiratory syncytial virus F and G proteins.Journal of virology · 2011Article
- Assembly and biological and immunological properties of Newcastle disease virus-like particles.Journal of virology · 2010Article
- Probing the spatial organization of measles virus fusion complexes.Journal of virology · 2009Article
- Role of thiol/disulfide exchange in newcastle disease virus entry.Journal of virology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Newcastle disease virus (NDV) fusion (F) protein directs membrane fusion, which is required for virus entry and cell-cell fusion. We have previously shown that free thiols are present in cell surface-expressed NDV F protein and that blocking the production of free thiols by thiol-disulfide exchange inhibitors inhibited the membrane fusion mediated by F protein (J Virol. 81:2328-2339, 2007). Extending these observations, we evaluated the role of the overexpression of two disulfide bond isomerases, protein disulfide isomerase (PDI) and ERdj5, in cell-cell fusion mediated by NDV glycoproteins. The overexpression of these isomerases resulted in significantly increased membrane fusion, as measured by syncytium formation and content mixing. The overexpression of these isomerases enhanced the production of free thiols in F protein when expressed without hemagglutination-neuraminidase (HN) protein but decreased free thiols in F protein expressed with HN protein. By evaluating the binding of conformation-sensitive antibodies, we found that the overexpression of these isomerases favored a postfusion conformation of surface-expressed F protein in the presence of HN protein. These results suggest that isomerases belonging to the PDI family catalyze the production of free thiols in F protein, and free thiols in F protein facilitate membrane fusion mediated by F protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.