ArticleJournal of virology2005
The fusion-controlling disulfide bond isomerase in retrovirus Env is triggered by protein destabilization.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Dynamics and Structural Responses to Cis-Trans Isomerization in Bacterial Lipid Bilayers.ACS omega · 2026Article
- Conserved residues of the immunosuppressive domain of MLV are essential for regulating the fusion-critical SU-TM disulfide bond.Journal of virology · 2024Article
- Characterization and application of recombinant Bovine Leukemia Virus Env protein.Scientific reports · 2024Article
- Reconstitution of Fusion-Competent Human Placental Fusogen Syncytin-2.The Journal of membrane biology · 2022Article
- Review
- Directed Molecular Evolution of an Engineered Gammaretroviral Envelope Protein with Dual Receptor Use Shows Stable Maintenance of Both Receptor Specificities.Journal of virology · 2016Article
- Mechanism of multivalent nanoparticle encounter with HIV-1 for potency enhancement of peptide triazole virus inactivation.The Journal of biological chemistry · 2015Article
- Library screening and receptor-directed targeting of gammaretroviral vectors.Future microbiology · 2013Review
- Poxvirus cell entry: how many proteins does it take?Viruses · 2012Review
- Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.Journal of virology · 2012Article
- Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion.The EMBO journal · 2008Article
- Highly specific inhibition of leukaemia virus membrane fusion by interaction of peptide antagonists with a conserved region of the coiled coil of envelope.Retrovirology · 2008Article
- Intersubunit disulfide isomerization controls membrane fusion of human T-cell leukemia virus Env.Journal of virology · 2008Article
- Nonhelical leash and alpha-helical structures determine the potency of a peptide antagonist of human T-cell leukemia virus entry.Journal of virology · 2008Article
- Stabilization of TM trimer interactions during activation of moloney murine leukemia virus Env.Journal of virology · 2008Article
- The MuLV 4070A G541R Env mutation decreases the stability and alters the conformation of the TM ectodomain.Virology · 2008Article
- Thermostabilizing mutations in reovirus outer-capsid protein mu1 selected by heat inactivation of infectious subvirion particles.Virology · 2007Article
- Characterization of a structural intermediate of flavivirus membrane fusion.PLoS pathogens · 2007Article
- Viral and cellular determinants involved in hepadnaviral entry.World journal of gastroenterology · 2007Review
- Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env.Journal of virology · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane fusion function of murine leukemia virus (MLV) is carried by the Env protein. This protein is composed of three SU-TM subunit complexes. The fusion activity is loaded into the transmembrane TM subunit and controlled by the peripheral, receptor-binding SU subunit. It is assumed that TM adopts a metastable conformation in the native Env and that fusion activation involves the folding of TM into a stable form. Activation is suppressed by the associated SU and triggered by its dissociation, which follows receptor binding. Recently we showed that the two subunits are disulfide linked and that SU dissociation and triggering of the fusion function are caused by a switch of the intersubunit disulfide into an intrasubunit disulfide isomer using an isomerization-active CWLC motif in SU (M. Wallin, M. Ekstrom, and H. Garoff, EMBO J. 23:54-65, 2004). In the present work we address how the SU disulfide isomerase is activated. Using Moloney MLV, we show that isomerization of the SU-TM disulfide bond can be triggered by heat, urea, or guanidinium hydrochloride. Such protein perturbation treatments also significantly increase the kinetics and efficiency of viral fusion. The threshold conditions for the effects on isomerization and fusion are virtually the same. This finding indicates that destabilization of interactions in the SU oligomer induces the disulfide bond isomerase and the subsequent activation of the fusion function in TM.
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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.