ArticleNature communications2015
Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 115 citations in OpenAlex.
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- An H5N1 clade 2.3.4.4b virus vaccine that elicits cross-protective antibodies against conserved domains of H5 and N1 glycoproteins.Nature communications · 2026Article
- Pre-existing cross-reactive immunity to highly pathogenic avian influenza 2.3.4.4b A(H5N1) virus in the United States.Nature communications · 2025Article
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- Understanding the landscape of cross-species transmission, epidemiology, phylogenetics, and antigenicity of HPAI strain A(H5N1) causing a recent outbreak in the USA.Journal, genetic engineering & biotechnology · 2025Article
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- Immunogenicity and protective efficacy of an intranasal neuraminidase-based influenza vaccine with bacterial cell membrane-derived adjuvants.NPJ vaccines · 2025Article
- Influenza neuraminidase active site proximity assay for rapid profiling of inhibitory antibodies and antigenic drift.NPJ vaccines · 2025Article
- Identification of a seasonal influenza vaccine-induced broadly protective neuraminidase antibody.The Journal of experimental medicine · 2025Article
- Fluorescence-barcoded cell lines stably expressing membrane-anchored influenza neuraminidases.Vaccine · 2025Article
- Drug-Fc conjugate CD388 targets influenza virus neuraminidase and is broadly protective in mice.Nature microbiology · 2025Article
- Influenza A Virus H7 nanobody recognizes a conserved immunodominant epitope on hemagglutinin head and confers heterosubtypic protection.Nature communications · 2025Article
- Phylogenetic analysis of swine influenza viruses circulating in slaughterhouses in Thanh Hoa province, Vietnam, during 2024 and early 2025.Open veterinary journal · 2025Article
- A human monoclonal antibody targeting the monomeric N6 neuraminidase confers protection against avian H5N6 influenza virus infection.Nature communications · 2024Article
- Multi-COBRA hemagglutinin formulated with cGAMP microparticles elicits protective immune responses against influenza viruses.mSphere · 2024Article
- Capsid virus-like particle display improves recombinant influenza neuraminidase antigen stability and immunogenicity in mice.iScience · 2024Article
- Protective human monoclonal antibodies target conserved sites of vulnerability on the underside of influenza virus neuraminidase.Immunity · 2024Article
- Multi-COBRA hemagglutinin formulated with cGAMP microparticles elicit protective immune responses against influenza viruses.bioRxiv : the preprint server for biology · 2024Article
- Antibody inhibition of influenza A virus assembly and release.Journal of virology · 2024Article
- Leveraging vaccination-induced protective antibodies to define conserved epitopes on influenza N2 neuraminidase.Immunity · 2023Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A(H1N1)pdm09 influenza A viruses predominated in the 2013-2014 USA influenza season, and although most of these viruses remain sensitive to Food and Drug Administration-approved neuraminidase (NA) inhibitors, alternative therapies are needed. Here we show that monoclonal antibody CD6, selected for binding to the NA of the prototypic A(H1N1)pdm09 virus, A/California/07/2009, protects mice against lethal virus challenge. The crystal structure of NA in complex with CD6 Fab reveals a unique epitope, where the heavy-chain complementarity determining regions (HCDRs) 1 and 2 bind one NA monomer, the light-chain CDR2 binds the neighbouring monomer, whereas HCDR3 interacts with both monomers. This 30-amino-acid epitope spans the lateral face of an NA dimer and is conserved among circulating A(H1N1)pdm09 viruses. These results suggest that the large, lateral CD6 epitope may be an effective target of antibodies selected for development as therapeutic agents against circulating H1N1 influenza viruses.
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