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    "description": "Influenza virus neuraminidase (NA) is a major antiviral drug target and has recently reemerged as a key target of antibody-mediated protective immunity. Here we show that recombinant NAs across non-bat subtypes adopt various tetrameric conformations, including an \u201copen\u201d state that may help explain poorly understood variations in NA stability across viral strains and subtypes. We use homology-directed protein design to uncover the structural principles underlying these distinct tetrameric conformations and stabilize multiple recombinant NAs in the \u201cclosed\u201d state, yielding two near-atomic\u00a0resolution structures of NA by cryo-EM. In addition to enhancing thermal stability, conformational stabilization improves affinity to protective antibodies elicited by viral infection, including antibodies targeting a quaternary epitope and the broadly conserved catalytic site. Stabilized NAs can also be integrated into viruses without affecting fitness. Our findings provide a deeper understanding of NA structure, stability, and antigenicity, and establish design strategies for reinforcing the conformational integrity of recombinant NA proteins.", 
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    "id": "sg:pub.10.1038/s41467-022-29416-z", 
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        "id": "sg:journal.1043282", 
        "issn": [
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        "name": "Nature Communications", 
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    ], 
    "keywords": [
      "tetrameric conformation", 
      "structure-based design", 
      "recombinant neuraminidase", 
      "antiviral drug target", 
      "resolution structure", 
      "cryo-EM", 
      "protein design", 
      "drug targets", 
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      "conformational integrity", 
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      "subtypes", 
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      "immunity", 
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      "antibody-mediated protective immunity", 
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      "infection", 
      "protective immunity", 
      "quaternary epitopes", 
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      "findings", 
      "state", 
      "design strategy", 
      "protective antibodies", 
      "thermal stability", 
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    "name": "Structure-based design of stabilized recombinant influenza neuraminidase tetramers", 
    "pagination": "1825", 
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