Researchers used cryo-EM and functional experiments to resolve how Andes hantavirus recognizes protocadherin-1 (PCDH1) at near-atomic detail. The study, published in Nature, clarifies the assembled viral spike architecture required for receptor engagement. Teams at Albert Einstein College of Medicine, Institut Pasteur, and LSU Health Shreveport showed that an isolated spike subunit could not bind PCDH1; instead, the binding pocket forms through the four-copy arrangement of Gn glycoproteins. Mutagenesis identified specific Gn loops that shape the receptor-binding site and also enabled transfer of binding capacity between New World and Old World hantavirus glycoproteins. The work also mapped how neutralizing antibodies interfere, either blocking access to the binding pocket or physically preventing receptor engagement. Those structural and mechanistic insights can inform antibody discovery and other entry-inhibition strategies.