National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
United States
Citation
Journal: Science / Year: 2022 Title: Architecture and antigenicity of the Nipah virus attachment glycoprotein. Authors: Zhaoqian Wang / Moushimi Amaya / Amin Addetia / Ha V Dang / Gabriella Reggiano / Lianying Yan / Andrew C Hickey / Frank DiMaio / Christopher C Broder / David Veesler / Abstract: Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness. The entry of HNVs into host cells requires the attachment ...Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness. The entry of HNVs into host cells requires the attachment (G) and fusion (F) glycoproteins, which are the main targets of antibody responses. To understand viral infection and host immunity, we determined a cryo-electron microscopy structure of the NiV G homotetrameric ectodomain in complex with the nAH1.3 broadly neutralizing antibody Fab fragment. We show that a cocktail of two nonoverlapping G-specific antibodies neutralizes NiV and HeV synergistically and limits the emergence of escape mutants. Analysis of polyclonal serum antibody responses elicited by vaccination of macaques with NiV G indicates that the receptor binding head domain is immunodominant. These results pave the way for implementing multipronged therapeutic strategies against these deadly pathogens.
History
Deposition
Feb 10, 2022
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Header (metadata) release
Mar 9, 2022
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Map release
Mar 9, 2022
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Update
Apr 20, 2022
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Current status
Apr 20, 2022
Processing site: RCSB / Status: Released
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