Journal: Nat Commun / Year: 2022 Title: Structure-based design of stabilized recombinant influenza neuraminidase tetramers. Authors: Daniel Ellis / Julia Lederhofer / Oliver J Acton / Yaroslav Tsybovsky / Sally Kephart / Christina Yap / Rebecca A Gillespie / Adrian Creanga / Audrey Olshefsky / Tyler Stephens / Deleah ...Authors: Daniel Ellis / Julia Lederhofer / Oliver J Acton / Yaroslav Tsybovsky / Sally Kephart / Christina Yap / Rebecca A Gillespie / Adrian Creanga / Audrey Olshefsky / Tyler Stephens / Deleah Pettie / Michael Murphy / Claire Sydeman / Maggie Ahlrichs / Sidney Chan / Andrew J Borst / Young-Jun Park / Kelly K Lee / Barney S Graham / David Veesler / Neil P King / Masaru Kanekiyo / Abstract: 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- ...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 "open" 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 "closed" state, yielding two near-atomic resolution 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.
Mass: 42577.742 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Influenza A virus / Production host: Homo sapiens (human)
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