ArticleThe EMBO journal2008
Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion.
Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Computational analysis of envelope glycoproteins from diverse geographical isolates of bovine leukemia virus identifies highly conserved peptide motifs.Retrovirology · 2018Article
- Sequential activation of the three protomers in the Moloney murine leukemia virus Env.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Native structure of a retroviral envelope protein and its conformational change upon interaction with the target cell.Journal of structural biology · 2017Article
- Furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Inhibition of the HIV-1 spike by single-PG9/16-antibody binding suggests a coordinated-activation model for its three protomeric units.Journal of virology · 2013Article
- Visualization of the two-step fusion process of the retrovirus avian sarcoma/leukosis virus by cryo-electron tomography.Journal of virology · 2012Article
- Maturation cleavage of the murine leukemia virus Env precursor separates the transmembrane subunits to prime it for receptor triggering.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Cooperative cleavage of the R peptide in the Env trimer of Moloney murine leukemia virus facilitates its maturation for fusion competence.Journal of virology · 2011Article
- Charge-surrounded pockets and electrostatic interactions with small ions modulate the activity of retroviral fusion proteins.PLoS pathogens · 2011Article
- Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Morphology and ultrastructure of retrovirus particles.AIMS biophysicsArticle
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of the membrane fusion protein Env of Moloney mouse leukaemia virus is controlled by isomerization of the disulphide that couples its transmembrane (TM) and surface (SU) subunits. We have arrested Env activation at a stage prior to isomerization by alkylating the active thiol in SU and compared the structure of isomerization-arrested Env with that of native Env. Env trimers of respective form were isolated from solubilized particles by sedimentation and their structures were reconstructed from electron microscopic images of both vitrified and negatively stained samples. We found that the protomeric unit of both trimers formed three protrusions, a top, middle and a lower one. The atomic structure of the receptor-binding domain of SU fitted into the upper protrusion. This was formed similar to a bent finger. Significantly, in native Env the tips of the fingers were directed against each other enclosing a cavity below, whereas they had turned outward in isomerization-arrested Env transforming the cavity into an open well. This might subsequently guide the fusion peptides in extended TM subunits into the target membrane.
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