Authors: Zhaoqian Wang, Moushimi Amaya, Amin Addetia, Ha V. Dang, Gabriella Reggiano, Lianying Yan, Andrew C. Hickey, Frank DiMaio, Christopher C. Broder, David Veesler
Year: 2022
Journal: Science
DOI: 10.1126/science.abm5561
Summary#
This paper determines a cryo-electron microscopy structure of the Nipah virus (NiV) attachment glycoprotein (G) homotetrameric ectodomain in complex with the nAH1.3 broadly neutralizing antibody Fab fragment. The results suggest a multi-pronged therapeutic strategy against these deadly pathogens.
Key Findings#
- A cocktail of two non-overlapping G-specific antibodies neutralizes NiV and HeV synergistically and limits the emergence of escape mutants.
- The receptor-binding head domain is immunodominant in polyclonal serum antibody responses elicited by vaccination of macaques with NiV G.
Methodology#
- Study Type: Laboratory Study
- Sample Size: N/A (experimental model study)
Topics#
Virology, Immunology
Relevance#
The results pave the way for implementing multi-pronged therapeutic strategies against deadly pathogens like Nipah and Hendra viruses.