ArticleJournal of virology2017
An Amino Acid in the Stalk Domain of N1 Neuraminidase Is Critical for Enzymatic Activity.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 41 citations in OpenAlex.
- Neuraminidase-on-a-string nanoparticles probe how antigenic distance shapes elicited humoral immunity.Research square · 2025Article
- Neuraminidase-on-a-string nanoparticles probe how antigenic distance shapes elicited humoral immunity.bioRxiv : the preprint server for biology · 2025Article
- Evolutionary dynamics and molecular epidemiology of H1N1 pandemic 2009 influenza A viruses across swine farms in Denmark.Virus evolution · 2025Article
- Dual neutralization of influenza virus hemagglutinin and neuraminidase by a bispecific antibody leads to improved antiviral activity.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Avian Influenza Virus Tropism in Humans.Viruses · 2023Review
- Phenotypic effects of mutations observed in the neuraminidase of human origin H5N1 influenza A viruses.PLoS pathogens · 2023Article
- Swine H1N1 Influenza Virus Variants with Enhanced Polymerase Activity and HA Stability Promote Airborne Transmission in Ferrets.Journal of virology · 2022Article
- Structure-based design of stabilized recombinant influenza neuraminidase tetramers.Nature communications · 2022Article
- Influenza A Virus Hemagglutinin-Neuraminidase-Receptor Balance: Preserving Virus Motility.Trends in microbiology · 2020Review
- Structural restrictions for influenza neuraminidase activity promote adaptation and diversification.Nature microbiology · 2019Article
- Tropism and Infectivity of a Seasonal A(H1N1) and a Highly Pathogenic Avian A(H5N1) Influenza Virus in Primary Differentiated Ferret Nasal Epithelial Cell Cultures.Journal of virology · 2019Article
- Influenza Virus Neuraminidase Structure and Functions.Frontiers in microbiology · 2019Review
- Inhibition of sialidase activity as a therapeutic approach.Drug design, development and therapy · 2018Review
- From Variation of Influenza Viral Proteins to Vaccine Development.International journal of molecular sciences · 2017Review
- Mutation of the Second Sialic Acid-Binding Site, Resulting in Reduced Neuraminidase Activity, Preceded the Emergence of H7N9 Influenza A Virus.Journal of virology · 2017Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Neuraminidase (NA) is a sialidase expressed on the surface of influenza A viruses that releases progeny viruses from the surface of infected cells and prevents viruses becoming trapped in mucus. It is a homotetramer, with each monomer consisting of a transmembrane region, a stalk, and a globular head with sialidase activity. We recently characterized two swine viruses of the pandemic H1N1 lineage, A/swine/Virginia/1814-1/2012 (pH1N1 IMPORTANCE: Neuraminidase (NA) is a sialidase that is one of the major surface glycoproteins of influenza A viruses and the target for the influenza drugs oseltamivir and zanamivir. NA is important as it releases progeny viruses from the surface of infected cells and prevents viruses becoming trapped in mucus. Mutations in the globular head domain that decrease enzymatic activity but confer resistance to NA inhibitors have been characterized; however, the importance of specific mutations in the stalk domain is unknown. We identified 66Y (N1 numbering), a highly conserved amino acid that was critical for the stability of the NA tetramer and, subsequently, for NA enzymatic activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.