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TitleStructure-based design of stabilized recombinant influenza neuraminidase tetramers.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1825, Year 2022
Publish dateApr 5, 2022
AuthorsDaniel 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 /
PubMed AbstractInfluenza 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.
External linksNat Commun / PubMed:35383176 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.25 Å
Structure data

26318

7u2q

EMDB-26318, PDB-7u2q:
Influenza Neuraminidase N1-CA09-sNAp-155
Method: EM (single particle) / Resolution: 3.2 Å

26319

7u2t

EMDB-26319, PDB-7u2t:
Influenza Neuraminidase N1-MI15-sNAp-174
Method: EM (single particle) / Resolution: 3.25 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • influenza a virus
KeywordsVIRAL PROTEIN / Influenza / Antigen / Engineered Protein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID

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