Complexity in Influenza Virus Targeted Drug Design: Interaction with Human Sialidases
Abstract
With the global spread of the pandemic H1N1 and the ongoing pandemic potential of the H5N1 subtype, the influenza virus represents one of the most alarming viruses spreading worldwide. The influenza virus sialidase is an effective drug target, and a number of inhibitors are clinically effective against the virus (zanamivir, oseltamivir, peramivir). Here we report structural and biochemical studies of the human cytosolic sialidase Neu2 with influenza virus sialidase-targeting drugs and related compounds.
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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 [75]
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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
- Chavas, L. M. G., Kato, R., Suzuki, N., von Itzstein, M., Mann, M. C., Thomson, R. J., Dyason, J. C., McKimm-Breschkin, J., Fusi, P., Tringali, C., Venerando, B., Tettamanti, G., Monti, E., & Wakatsuki, S.
- Affiliations
- High Energy Accelerator Research Organization (JP)
- Griffith University (AU)
- University of Milano-Bicocca (IT)
- University of Milan (IT)
- University of Brescia (IT)
- ORCID
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-04-08
- Volume
- 53
- Issue
- 7
- Pages
- 2998-3002
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W1988280153
- Cited by
- 68
- References
- 0
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 4 · 2014: 9 · 2013: 5 · 2012: 9
- FWCI
- 7.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion)
- Griffith Research Online (submittedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- influenza virus, neuraminidase, NEU2, sialidase inhibitors, drug design, zanamivir, oseltamivir, peramivir, H1N1 pandemic, H5N1, structure-activity relationship, antiviral drug targets
- MeSH terms
- Enzyme Inhibitors, Humans, Models, Molecular, Molecular Conformation, Neuraminidase, Orthomyxoviridae, Drug Design, Crystallography, X-Ray, Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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