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6TYS

A potent cross-neutralizing antibody targeting the fusion glycoprotein inhibits Nipah virus and Hendra virus infection

Summary for 6TYS
Entry DOI10.2210/pdb6tys/pdb
EMDB information20584
DescriptorFusion glycoprotein F0, 5B3 antibody heavy chain, 5B3 antibody light chain, ... (7 entities in total)
Functional Keywordshenipavirus, nipah virus, hendra virus, fusion glycoprotein, antibody, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein-immune system complex, viral protein/immune system
Biological sourceNipah virus
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Total number of polymer chains9
Total formula weight261038.15
Authors
Primary citationDang, H.V.,Chan, Y.P.,Park, Y.J.,Snijder, J.,Da Silva, S.C.,Vu, B.,Yan, L.,Feng, Y.R.,Rockx, B.,Geisbert, T.W.,Mire, C.E.,Broder, C.C.,Veesler, D.
An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections.
Nat.Struct.Mol.Biol., 26:980-987, 2019
Cited by
PubMed Abstract: Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness with fatality rates of 50-100%. No vaccines or licensed therapeutics currently exist to protect humans against NiV or HeV. HNVs enter host cells by fusing the viral and cellular membranes via the concerted action of the attachment (G) and fusion (F) glycoproteins, the main targets of the humoral immune response. Here, we describe the isolation and humanization of a potent monoclonal antibody cross-neutralizing NiV and HeV. Cryo-electron microscopy, triggering and fusion studies show the antibody binds to a prefusion-specific quaternary epitope, conserved in NiV F and HeV F glycoproteins, and prevents membrane fusion and viral entry. This work supports the importance of the HNV prefusion F conformation for eliciting a robust immune response and paves the way for using this antibody for prophylaxis and post-exposure therapy with NiV- and HeV-infected individuals.
PubMed: 31570878
DOI: 10.1038/s41594-019-0308-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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