Nature Communications (Apr 2022)
Structure-based design of stabilized recombinant influenza neuraminidase tetramers
- 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
Affiliations
- Daniel Ellis
- Institute for Protein Design, University of Washington
- Julia Lederhofer
- Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- Oliver J. Acton
- Department of Biochemistry, University of Washington
- Yaroslav Tsybovsky
- Electron Microscopy Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute
- Sally Kephart
- Department of Medicinal Chemistry, University of Washington
- Christina Yap
- Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- Rebecca A. Gillespie
- Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- Adrian Creanga
- Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- Audrey Olshefsky
- Institute for Protein Design, University of Washington
- Tyler Stephens
- Electron Microscopy Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute
- Deleah Pettie
- Institute for Protein Design, University of Washington
- Michael Murphy
- Institute for Protein Design, University of Washington
- Claire Sydeman
- Institute for Protein Design, University of Washington
- Maggie Ahlrichs
- Institute for Protein Design, University of Washington
- Sidney Chan
- Institute for Protein Design, University of Washington
- Andrew J. Borst
- Institute for Protein Design, University of Washington
- Young-Jun Park
- Department of Biochemistry, University of Washington
- Kelly K. Lee
- Department of Medicinal Chemistry, University of Washington
- Barney S. Graham
- Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- David Veesler
- Department of Biochemistry, University of Washington
- Neil P. King
- Institute for Protein Design, University of Washington
- Masaru Kanekiyo
- Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
- DOI
- https://doi.org/10.1038/s41467-022-29416-z
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 16
Abstract
Influenza virus neuraminidase (NA) is a drug target and a potential vaccine antigen. Here, the authors provide a detailed analysis of the conformational stability of NA, and show how expression and stability of recombinant NA antigens can be strengthened through structure-based design.
