The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells
Open accessPreprint — published as 10.1038/s41467-023-36923-0 · Paper page
Abstract
The surface envelope glycoprotein (Env) of all retroviruses mediates virus binding to cells and fusion of the viral and cellular membranes. A structure-function relationship for the HIV Env that belongs to the Orthoretrovirus subfamily has been well established. Structural information is however largely missing for the Env of Foamy viruses (FVs), the second retroviral subfamily. FV Envs lack sequence similarity with their HIV counterpart. We present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.6 Å resolution, revealing two subdomains and an unprecedented fold. We have generated a model for the organization of the RBDs within the trimeric Env which indicates that the upper subdomain is important for stabilization of the full-length Env, and have demonstrated that residues K342, R343, R359 and R369 in the lower subdomain play key roles in the interaction of the RBD and viral particles with heparan sulfate.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Fernández, I., Dynesen, L. T., Coquin, Y., Pederzoli, R., Brun, D., Haouz, A., Gessain, A., Rey, F., Buseyne, F., & Backovic, M.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institut Pasteur
- ORCID
- Venue
- Nature Communications
- Published
- 2022-10-17
- Volume
- 14
- Issue
- 1
- Pages
- 1262-1262
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9988990
- OpenAlex
- W4323310853
- Cited by
- 11
- References
- 1
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 3 · 2023: 2
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agence Nationale de la Recherche (ANR‐10‐LABX‐62‐IBEID, ANR-10, ANR-10-LABX-0062)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- simian foamy virus, receptor binding domain, envelope glycoprotein, viral entry, host cell receptors, heparan sulfate, cage-like structure, X-ray crystal structure
- MeSH terms
- Cell Membrane, Membrane Glycoproteins, Retroviridae, Spumavirus, Simian foamy virus
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