The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

Ignacio Fernández, Lasse Toftdal Dynesen, Youna Coquin, Riccardo Pederzoli, Delphine Brun, Ahmed Haouz, Antoine Gessain, Félix A. Rey, Florence Buseyne and Marija Backovic ()
Additional contact information
Ignacio Fernández: Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale
Lasse Toftdal Dynesen: Université Paris Cité, CNRS UMR3569, Unité d’Épidémiologie et Physiopathologie des Virus Oncogènes
Youna Coquin: Université Paris Cité, CNRS UMR3569, Unité d’Épidémiologie et Physiopathologie des Virus Oncogènes
Riccardo Pederzoli: Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale
Delphine Brun: Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale
Ahmed Haouz: Université Paris Cité, Plateforme de cristallographie-C2RT, CNRS UMR 3528
Antoine Gessain: Université Paris Cité, CNRS UMR3569, Unité d’Épidémiologie et Physiopathologie des Virus Oncogènes
Félix A. Rey: Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale
Florence Buseyne: Université Paris Cité, CNRS UMR3569, Unité d’Épidémiologie et Physiopathologie des Virus Oncogènes
Marija Backovic: Université Paris Cité, CNRS UMR3569, Unité de Virologie Structurale

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: 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. In this work we present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.57 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 subdomains form a cage-like structure at the apex of the Env, and identified residues K342, R343, R359 and R369 in the lower subdomain as key players for the interaction of the RBD and viral particles with heparan sulfate.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-36923-0 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36923-0

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-36923-0

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().