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Structure paper

TitleStructural basis for antibody recognition of vulnerable epitopes on Nipah virus F protein.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 1494, Year 2023
Publish dateMar 17, 2023
AuthorsPatrick O Byrne / Brian E Fisher / David R Ambrozak / Elizabeth G Blade / Yaroslav Tsybovsky / Barney S Graham / Jason S McLellan / Rebecca J Loomis /
PubMed AbstractNipah virus (NiV) is a pathogenic paramyxovirus that causes fatal encephalitis in humans. Two envelope glycoproteins, the attachment protein (G/RBP) and fusion protein (F), facilitate entry into host ...Nipah virus (NiV) is a pathogenic paramyxovirus that causes fatal encephalitis in humans. Two envelope glycoproteins, the attachment protein (G/RBP) and fusion protein (F), facilitate entry into host cells. Due to its vital role, NiV F presents an attractive target for developing vaccines and therapeutics. Several neutralization-sensitive epitopes on the NiV F apex have been described, however the antigenicity of most of the F protein's surface remains uncharacterized. Here, we immunize mice with prefusion-stabilized NiV F and isolate ten monoclonal antibodies that neutralize pseudotyped virus. Cryo-electron microscopy reveals eight neutralization-sensitive epitopes on NiV F, four of which have not previously been described. Novel sites span the lateral and basal faces of NiV F, expanding the known library of vulnerable epitopes. Seven of ten antibodies bind the Hendra virus (HeV) F protein. Multiple sequence alignment suggests that some of these newly identified neutralizing antibodies may also bind F proteins across the Henipavirus genus. This work identifies new epitopes as targets for therapeutics, provides a molecular basis for NiV neutralization, and lays a foundation for development of new cross-reactive antibodies targeting Henipavirus F proteins.
External linksNat Commun / PubMed:36932063 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.0 Å
Structure data

26652

7uop

EMDB-26652, PDB-7uop:
Prefusion-stabilized Nipah virus fusion protein complexed with Fab 4H3
Method: EM (single particle) / Resolution: 2.8 Å

26658

7up9

EMDB-26658, PDB-7up9:
Prefusion-stabilized Nipah virus fusion protein complexed with Fab 2D3
Method: EM (single particle) / Resolution: 2.9 Å

26659

7upa

EMDB-26659, PDB-7upa:
Prefusion-stabilized Nipah virus fusion protein complexed with Fab 1H8
Method: EM (single particle) / Resolution: 2.5 Å

26660

7upb

EMDB-26660, PDB-7upb:
Prefusion-stabilized Nipah virus fusion protein complexed with Fab 1H1
Method: EM (single particle) / Resolution: 3.0 Å

26662

7upd

EMDB-26662, PDB-7upd:
Prefusion-stabilized Nipah virus fusion protein complexed with Fab 2B12
Method: EM (single particle) / Resolution: 2.4 Å

26668

7upk

EMDB-26668, PDB-7upk:
Prefusion-stabilized Nipah virus fusion protein complexed with Fab 1A9
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • nipah henipavirus
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN/Immune System / Henipavirus / Nipah virus / NiV / F / fusion / prefusion / preF / pre-F / neutralizing antibody / Fab / VIRAL PROTEIN / VIRAL PROTEIN-Immune System complex

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