Structural highlights
FunctionPublication Abstract from PubMedAfrican horse sickness virus (AHSV) is a lethal equine pathogen with no licensed vaccine other than vaccines containing attenuated virus, which pose safety risks. Endemic to sub-Saharan Africa, AHSV has caused epizootics in Spain and Portugal, Cyprus, Morocco, the Middle East, India and Pakistan and, most recently, Thailand. Here, we resolve the 3.11 A cryo-EM structure of full-length VP2 from AHSV serotype 4, adopting its native triskelion architecture and shedding light on an alpha-helical domain anchoring the triskelion core, which is absent in other structurally characterized orbiviruses. Structure-guided mapping identified a subdomain of VP2 as a key target of neutralizing antibodies. Displayed on nanoparticles using the SpyCatcher/SpyTag technology, the domain conferred complete protection from clinical disease after viral challenge infection in mice and elicited robust and long-lasting immune responses in horses, the target species of AHSV. These findings provide a structural blueprint for the next generation of recombinant vaccines against AHSV and related orbiviruses. Cryo-EM structure of African horse sickness virus VP2 receptor-binding protein enables nanoparticle vaccine design.,Martinez-Castillo A, Aebischer A, Toneatti P, Fu L, Vitour D, Sailleau C, Hoffmann B, Franzke K, Eschbaumer M, Weber S, Calvo Pinilla E, Ortego J, Gil-Carton D, Breard E, Zientara S, Kortekaas J, Beer M, Abrescia NG Nat Commun. 2026 Jul 4. doi: 10.1038/s41467-026-75067-9. PMID:42401561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 16:20, 22 July 2026.