9HBP
Cryo-EM structure of the canine distemper virus tetrameric attachment H glycoprotein in complex with two different Nanobodies
This is a non-PDB format compatible entry.
Summary for 9HBP
| Entry DOI | 10.2210/pdb9hbp/pdb |
| EMDB information | 52024 |
| Descriptor | Hemagglutinin glycoprotein, Nanobody H7, Nanobody H9, ... (4 entities in total) |
| Functional Keywords | canine distemper virus, hemagglutinine, cdv, h-protein, complex, nanobody, viral protein |
| Biological source | Morbillivirus canis More |
| Total number of polymer chains | 12 |
| Total formula weight | 382646.65 |
| Authors | |
| Primary citation | Scherer, M.,Djabeur, N.,Siering, O.,Jeckelmann, J.M.,Wyss, M.,Cresci, M.,Di Palma Subran, M.,Riedl, R.,Chames, P.,Pfaller, C.K.,Sawatsky, B.,Fotiadis, D.,Plattet, P. Protection against lethal canine distemper virus infection by a dual epitope-targeting synthetic antibody. Nat Commun, 17:103-103, 2026 Cited by PubMed Abstract: Despite vaccine availability, the morbilliviruses measles virus and canine distemper virus (CDV) are still causing major health impairments in human and animal populations. Here, we identified two potent, neutralizing single domain antibodies directed against the tetrameric receptor binding (H) protein of CDV. Structural analyses spotlighted two vulnerable sites within the H protein. While the first overlaps with the receptor binding site, the second encompasses amino acid residues of two protomers located at the distal dimeric head interface, which supports distinct mechanisms of neutralization. Upon application of an engineered tetravalent and biparatopic antibody, ferrets were protected at a remarkably low antibody dose (1 mg/kg) administered intra-peritoneally on days 3 and 7 post-exposure of a lethal CDV challenge. Collectively, this study spotlights the power of integrating multiple mechanisms of neutralization in a single format and provides a roadmap to design next-generation therapeutics against morbilliviral infections as well as other infectious pathogens. PubMed: 41501035DOI: 10.1038/s41467-025-67600-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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