8RM1
Cryo-EM structure of a Foamy Virus fusion glycoprotein in the postfusion conformation
Summary for 8RM1
Entry DOI | 10.2210/pdb8rm1/pdb |
EMDB information | 19348 |
Descriptor | Envelope glycoprotein gp130, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | envelope, fusion, spumavirus, virus |
Biological source | Simian foamy virus More |
Total number of polymer chains | 6 |
Total formula weight | 286052.84 |
Authors | Fernandez, I.,Backovic, M. (deposition date: 2024-01-04, release date: 2024-10-23, Last modification date: 2024-11-20) |
Primary citation | Fernandez, I.,Bontems, F.,Brun, D.,Coquin, Y.,Goverde, C.A.,Correia, B.E.,Gessain, A.,Buseyne, F.,Rey, F.A.,Backovic, M. Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses. Sci Adv, 10:eado7035-eado7035, 2024 Cited by PubMed Abstract: Foamy viruses (FVs) constitute a subfamily of retroviruses. Their envelope (Env) glycoprotein drives the merger of viral and cellular membranes during entry into cells. The only available structures of retroviral Envs are those from human and simian immunodeficiency viruses from the subfamily of orthoretroviruses, which are only distantly related to the FVs. We report the cryo-electron microscopy structures of the FV Env ectodomain in the pre- and post-fusion states, which unexpectedly demonstrate structural similarity with the fusion protein (F) of paramyxo- and pneumoviruses, implying an evolutionary link between the viral fusogens. We describe the structural features that are unique to the FV Env and propose a mechanistic model for its conformational change, highlighting how the interplay of its structural elements could drive membrane fusion and viral entry. The structural knowledge on the FV Env now provides a framework for functional investigations, which can benefit the design of FV Env variants with improved features for use as gene therapy vectors. PubMed: 39392890DOI: 10.1126/sciadv.ado7035 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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