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TitleAntigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species.
Journal, issue, pagesNPJ Vaccines, Vol. 11, Issue 1, Page 5, Year 2025
Publish dateNov 28, 2025
AuthorsDan Zhou / Yong Wang / Yanfeng Yao / Wenhua Kuang / Rao Cheng / Gan Zhang / Hang Liu / Xin Li / Sandra Chiu / Zengqin Deng / Haiyan Zhao /
PubMed AbstractNipah virus (NiV) and Hendra virus (HeV), two highly pathogenic Henipaviruses (HNVs), pose a significant public health threat. The attachment glycoprotein (G) plays a crucial role in viral attachment ...Nipah virus (NiV) and Hendra virus (HeV), two highly pathogenic Henipaviruses (HNVs), pose a significant public health threat. The attachment glycoprotein (G) plays a crucial role in viral attachment and entry, making it an attractive target for vaccine and therapeutic antibody development. However, the antigenic landscape and neutralization sensitivity of the diverse HNV G proteins remain poorly defined. Here, we systematically characterize 27 monoclonal antibodies (mAbs) elicited by NiV G head (G) nanoparticle-immunized mice. Among these, 25 mAbs exhibit neutralizing activity against two major NiV strains, NiV-Malaysia and NiV-Bangladesh, with five mAbs also cross-inhibiting HeV infection. Notably, mAbs from two distinct groups conferred complete protection to hamsters against lethal NiV-Malaysia challenge. Structural analysis of NiV G in complex with representative Fabs reveals four non-overlapping epitopes, including two novel antigenic sites and one public protective epitope shared across species. MAbs targeting the novel sites bind to the top or side faces of G protein's β-propeller and inhibit viral infection by blocking either receptor engagement or membrane fusion. MAbs recognizing the public epitope block the receptor binding directly. Our study provides a comprehensive antigenic map of the NiV G and offers new insights and opportunities for antibody-based therapies and rational vaccine development.
External linksNPJ Vaccines / PubMed:41315143 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3 - 3.03 Å
Structure data

63395

9lue

EMDB-63395, PDB-9lue:
Cryo-EM structure of the Nipah G head domain in complex with three Fabs
Method: EM (single particle) / Resolution: 3.03 Å

PDB-9lu3:
LN1F9 Fab bound to Nipah Virus attachment (G) glycoprotein head domain
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • henipavirus nipahense
  • mesocricetus auratus (golden hamster)
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Glycoprotein G / Fab / VIRAL PROTEIN-IMMUNE SYSTEM complex / Nipah G protein / Antibodies

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