9OC6
Crystal structure of receptor FcRn bound to Human Astrovirus 6 spike
Summary for 9OC6
| Entry DOI | 10.2210/pdb9oc6/pdb |
| Descriptor | IgG receptor FcRn large subunit p51, Beta-2-microglobulin, Capsid polyprotein VP90 (3 entities in total) |
| Functional Keywords | astrovirus, fcrn, virus host interaction, hastv, immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 70085.64 |
| Authors | Agrawal, S.,Wilson, I.A. (deposition date: 2025-04-23, release date: 2025-11-19, Last modification date: 2025-12-24) |
| Primary citation | Agrawal, S.,Jain, M.,Marinelli, D.,Cho, S.Y.,Briney, B.,Wilson, I.A. Structural hijacking of FcRn by human astrovirus spikes reveals conserved epitopes for broad-spectrum antivirals. Cell Rep, 44:116679-116679, 2025 Cited by PubMed Abstract: Human astroviruses (HAstVs) are a leading cause of pediatric gastroenteritis and emerging systemic infections; however, no targeted therapies exist. A critical barrier to intervention has been the lack of molecular insights into viral entry, particularly the interaction between the HAstV capsid spike and its receptor, the neonatal Fc receptor (FcRn). Here, we report crystal structures of the HAstV spike from classical serotypes 2 and 6 in complex with human FcRn at 3 Å resolution, defining a conserved receptor-binding interface at atomic resolution. These structures reveal serotype-specific variations that dictate receptor affinity and demonstrate that reported neutralizing antibodies can inhibit infection by sterically blocking the receptor-binding site. Mapping conserved epitopes across classical HAstV serotypes provides a blueprint for designing broad-spectrum antivirals that disrupt viral entry. Notably, our structural data rationalize the potential repurposing of clinical FcRn inhibitors, such as nipocalimab, to block HAstV infection, bridging critical gaps in astrovirus biology and antiviral development. PubMed: 41389202DOI: 10.1016/j.celrep.2025.116679 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.97 Å) |
Structure validation
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