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-Structure paper
タイトル | Architecture and antigenicity of the Nipah virus attachment glycoprotein. |
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ジャーナル・号・ページ | Science, Vol. 375, Issue 6587, Page 1373-1378, Year 2022 |
掲載日 | 2022年3月25日 |
著者 | Zhaoqian Wang / Moushimi Amaya / Amin Addetia / Ha V Dang / Gabriella Reggiano / Lianying Yan / Andrew C Hickey / Frank DiMaio / Christopher C Broder / David Veesler / |
PubMed 要旨 | 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. |
リンク | Science / PubMed:35239409 |
手法 | EM (単粒子) |
解像度 | 3.2 - 3.5 Å |
構造データ | EMDB-26162, PDB-7txz: EMDB-26163, PDB-7ty0: EMDB-26164: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN / NiV / NiVG / attachment protein / neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID |