Structures of the Foamy virus fusion protein reveal an unexpected link with the F protein of paramyxo- and pneumoviruses.
Autor: | Fernández I; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale, 75015 Paris, France., Bontems F; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale, 75015 Paris, France.; Institut de Chimie des Substances Naturelles, CNRS UPR2301, Université Paris Saclay, 91190 Gif-sur-Yvette, France., Brun D; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale, 75015 Paris, France., Coquin Y; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité d'Epidémiologie et Physiopathologie des Virus Oncogènes, 75015 Paris, France., Goverde CA; Institute of Bioengineering, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland., Correia BE; Institute of Bioengineering, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland., Gessain A; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité d'Epidémiologie et Physiopathologie des Virus Oncogènes, 75015 Paris, France., Buseyne F; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité d'Epidémiologie et Physiopathologie des Virus Oncogènes, 75015 Paris, France., Rey FA; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale, 75015 Paris, France., Backovic M; Institut Pasteur, Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale, 75015 Paris, France. |
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Jazyk: | angličtina |
Zdroj: | Science advances [Sci Adv] 2024 Oct 11; Vol. 10 (41), pp. eado7035. Date of Electronic Publication: 2024 Oct 11. |
DOI: | 10.1126/sciadv.ado7035 |
Abstrakt: | 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. |
Databáze: | MEDLINE |
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