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

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 angstrom 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. Foamy viruses are ancient retroviruses that are prevalent in non-human primates. Fernandez et al. report an X-ray structure of a protein domain from a simian Foamy virus that mediates the attachment to cells, providing insights into viral entry.

Automated summary

This paper presents the X-ray structure of the receptor binding domain (RBD) from a simian Foamy virus, providing insights into the viral entry mechanism.