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- PDB-9nz0: Cryo-EM structure of vaccine elicited antibody 22F5 bound to the ... -

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Basic information

Entry
Database: PDB / ID: 9nz0
TitleCryo-EM structure of vaccine elicited antibody 22F5 bound to the post-fusion conformation of the LayV-F glycoprotein
Components
  • 22F5 Heavy Chain
  • 22F5 Kappa Light Chain
  • Fusion glycoprotein F0
KeywordsIMMUNE SYSTEM/VIRAL PROTEIN / Henipavirus / Langya virus / vaccine-elicited antibody / DII domain / shrew-origin / ANTIVIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN complex
Function / homologyPrecursor fusion glycoprotein F0, Paramyxoviridae / Fusion glycoprotein F0 / fusion of virus membrane with host plasma membrane / viral envelope / symbiont entry into host cell / host cell plasma membrane / virion membrane / Fusion glycoprotein F0
Function and homology information
Biological speciesLangya virus
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.31 Å
AuthorsKumar, U. / May, A. / Acharya, P.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Nat Commun / Year: 2026
Title: Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.
Authors: Aaron J May / Muralikrishna Lella / Jared Lindenberger / Alex Berkman / Ujjwal Kumar / Kejun Liu / Moumita Dutta / Maggie Barr / Rob Parks / Xiaozhi Lu / Madison Berry / Amanda Powell / ...Authors: Aaron J May / Muralikrishna Lella / Jared Lindenberger / Alex Berkman / Ujjwal Kumar / Kejun Liu / Moumita Dutta / Maggie Barr / Rob Parks / Xiaozhi Lu / Madison Berry / Amanda Powell / Amelia G Thompson / Sravya Sowdamini Nakka / Camila T França / Xiao Huang / Arpita Mrigwani / Kijun Song / Victor Ilevbare / Salam Sammour / Chan Soo Park / Radha Devkota Adhikari / Priyanka Devkota / Katarzyna Janowska / Yanshun Liu / Garrett Scapellato / Taylor N Spence / Katayoun Mansouri / Kevin Wiehe / Nancy J Sullivan / Rosemarie Mason / Robert J Edwards / Kevin O Saunders / Barton F Haynes / Priyamvada Acharya /
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 ...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.
History
DepositionMar 31, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 17, 2026Provider: repository / Type: Initial release
Revision 1.1Jul 1, 2026Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Fusion glycoprotein F0
B: Fusion glycoprotein F0
C: Fusion glycoprotein F0
D: 22F5 Heavy Chain
E: 22F5 Kappa Light Chain
F: 22F5 Heavy Chain
G: 22F5 Kappa Light Chain
H: 22F5 Kappa Light Chain
I: 22F5 Heavy Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)328,29315
Polymers326,9669
Non-polymers1,3276
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Fusion glycoprotein F0


Mass: 61468.840 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Langya virus / Production host: Homo sapiens (human) / References: UniProt: A0AAX3C923
#2: Antibody 22F5 Heavy Chain


Mass: 23195.980 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
#3: Antibody 22F5 Kappa Light Chain


Mass: 24323.928 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSource
1Complex of Langya virus F protein trimer with 22F5 fabCOMPLEX#1-#30MULTIPLE SOURCES
2Langya virus F proteinCOMPLEX#11RECOMBINANT
322F5 fabCOMPLEX#2-#31NATURAL
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
22Langya virus2971765
33Mus musculus (house mouse)10090
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2800 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 59.6 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.31 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 271130 / Symmetry type: POINT

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