Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
Abstract
The influenza virus neuraminidase glycoprotein is a tetramer with a box-shaped head, 100 X 100 X 60 A, attached to a slender stalk. The three-dimensional structure of neuraminidase heads shows that each monomer is composed of six topologically identical beta-sheets arranged in a propeller formation. The tetrameric enzyme has circular 4-fold symmetry stabilized in part by metal ions bound on the symmetry axis. Sugar residues are attached to four of the five potential glycosylation sequences, and in one case contribute to the interaction between subunits in the tetramer.
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The β-propeller fold of NEU1 is typical of viral and bacterial sialidases.
“This fold is typical of viral and bacterial sialidases (62, 63).”
From Structure of the immunoregulatory sialidase NEU1 (2023) · cites this paper as [62]
The NEU1 oligomerization mode is unrelated to viral sialidase tetramers, disulfide-mediated NEU3 dimers, or the various lattice interfaces observed in NEU2 crystal structures.
“The NEU1 oligomerization mode is unrelated to viral sialidase tetramers (62), disulfide-mediated NEU3 dimers (9), or the various lattice interfaces observed in NEU2 crystal structures (11, 75, 76), raising the possibility that NEU1 self-association may be required for complex formation with CTSA.”
From Structure of the immunoregulatory sialidase NEU1 (2023) · cites this paper as [62]
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Rational design of potent sialidase-based inhibitors of influenza virus replication
von Itzstein, M., Wu, W.-Y., Kok, G. B., Pegg, M. S., Dyason, J. C., Jin, B., Van Phan, T., Smythe, M. L., White, H. F., Oliver, S. W., et al. (1993) · Nature · doi:10.1038/363418a0 · Cited by 1,862 · see citing works
Self-citationBerks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596 · see citing works
Crennell, S., Garman, E., Laver, G., Vimr, E., & Taylor, G. (1994) · Structure · doi:10.1016/s0969-2126(00)00053-8 · Cited by 205 · see citing works
Sialic acid recognition by Vibrio cholerae neuraminidase
Moustafa, I., Connaris, H., Taylor, M., Zaitsev, V., Wilson, J. C., Kiefel, M. J., von Itzstein, M., & Taylor, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404965200 · Cited by 165 · see citing works
Structure of the immunoregulatory sialidase NEU1
Gorelik, A., Illes, K., Mazhab-Jafari, M. T., & Nagar, B. (2023) · Science Advances · doi:10.1126/sciadv.adf8169 · Cited by 36 · see citing works
- Authors
- Varghese, J. N., Laver, W. G., & Colman, P. M.
- Affiliations
- Commonwealth Scientific and Industrial Research Organisation (AU)
- Venue
- Nature
- Published
- 1983-05
- Volume
- 303
- Issue
- 5912
- Pages
- 35-40
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2071138716
- Cited by
- 891
- References
- 0
- Citations by year
- 2026: 11 · 2025: 13 · 2024: 16 · 2023: 14 · 2022: 10 · 2021: 18 · 2020: 7 · 2019: 9 · 2018: 17 · 2017: 15 · 2016: 12 · 2015: 15 · 2014: 27 · 2013: 30 · 2012: 25
- FWCI
- 31.73
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- influenza neuraminidase, glycoprotein structure, tetrameric enzyme, propeller structure, beta-sheet, metal ion binding, glycosylation, subunit interactions, 4-fold symmetry, protein crystal structure
- MeSH terms
- Antigens, Viral, Calcium, Disulfides, Glycoproteins, Membrane Proteins, Molecular Weight, Neuraminidase, Orthomyxoviridae, Protein Conformation, X-Ray Diffraction
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