Researchers at Albert Einstein College of Medicine, Institut Pasteur, and LSU Health Shreveport resolved near-atomic details of how Andes hantavirus engages the human receptor protocadherin-1 (PCDH1). In a Nature paper, the team combined cryo-electron microscopy, functional assays, and an AI-designed scaffold to stabilize the assembled viral spike complex outside the virus for structural analysis. They found PCDH1 binds asymmetrically within a deep central pocket formed by four copies of the viral Gn glycoprotein. Mutagenesis experiments identified three Gn loops shaping the binding site and showed the binding interface can be transferred across New World and Old World hantavirus glycoproteins. Structural and functional work on neutralizing antibodies indicated two mechanisms of blockade—either obstructing access to the pocket or creating a physical barrier to receptor engagement. The study offers a concrete structural target set for designing receptor-blocking interventions and for interpreting why Andes virus attachment may differ among hantavirus lineages.