9NZ0

Cryo-EM structure of vaccine elicited antibody 22F5 bound to the post-fusion conformation of the LayV-F glycoprotein

Summary for 9NZ0

• Entry DOI: 10.2210/pdb9nz0/pdb
• EMDB information: 48715
• Descriptor: Fusion glycoprotein F0, 22F5 Heavy Chain, 22F5 Kappa Light Chain, ... (4 entities in total)
• Functional Keywords: henipavirus, langya virus, vaccine-elicited antibody, dii domain, shrew-origin, antiviral protein, immune system-viral protein complex, immune system/viral protein
• Biological source: Langya virus; More
• Total number of polymer chains: 9
• Total formula weight: 328293.49

Authors

Kumar, U.,May, A.,Acharya, P. (deposition date: 2025-03-31, release date: 2026-06-17, Last modification date: 2026-07-01)

Primary citation

May, A.J.,Lella, M.,Lindenberger, J.,Berkman, A.,Kumar, U.,Liu, K.,Dutta, M.,Barr, M.,Parks, R.,Lu, X.,Berry, M.,Powell, A.,Thompson, A.G.,Sowdamini Nakka, S.,Franca, C.T.,Huang, X.,Mrigwani, A.,Song, K.,Ilevbare, V.,Sammour, S.,Park, C.S.,Devkota Adhikari, R.,Devkota, P.,Janowska, K.,Liu, Y.,Scapellato, G.,Spence, T.N.,Mansouri, K.,Wiehe, K.,Sullivan, N.J.,Mason, R.,Edwards, R.J.,Saunders, K.O.,Haynes, B.F.,Acharya, P.
Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.
Nat Commun, 2026

PubMed Abstract: Henipaviruses, in the Paramyxoviridae family, includes the highly virulent Nipah virus that causes reoccurring outbreaks of deadly disease. Recent discoveries of Henipavirus-like species, including the zoonotic Langya virus, have revealed much higher antigenic diversity than currently characterized and prompted the reorganization of these viruses into the Henipavirus and Parahenipavirus genera. Here, to explore the limits of structural and antigenic variation in both genera, collectively referred to as HNVs, we construct an expanded, diverse panel of HNV fusion and attachment glycoproteins from non-redundant HNV strains that better reflect global HNV diversity. We express and purify the fusion protein ectodomains and the attachment protein head domains and study their biochemical and biophysical properties. We perform immunization experiments in mice, eliciting antibodies reactive to multiple HNV fusion proteins. Cryo-electron microscopy structures elucidate molecular determinants of differential pre-fusion state stability and higher order contacts. A crystal structure of the Gamak virus attachment head domain reveals an additional domain appended to the conserved 6-bladed, β-propeller fold. Taken together, these studies expand the known structural and antigenic limits of the HNVs, reveal cross-reactive epitopes within both genera and provide foundational data for the development of broadly reactive countermeasures.

PubMed: 42321170
DOI: 10.1038/s41467-026-74212-8

Experimental method

ELECTRON MICROSCOPY (3.31 Å)