ArticleAntiviral research2016
An influenza A virus (H7N9) anti-neuraminidase monoclonal antibody with prophylactic and therapeutic activity in vivo.
Article in Antiviral research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 36 citations in OpenAlex.
- A monoclonal antibody-based, time-resolved fluorescence microsphere immunochromatographic testing strip for rapid and sensitive detection of H7 avian influenza viruses.BMC veterinary research · 2026Article
- Cross-protective efficacy of NA-based mRNA vaccine candidates against seasonal and avian influenza viruses.Frontiers in microbiology · 2026Article
- Catch, Cut, or Block? Versatile 4-N-Derivatized Sialyl Glycosides for Influenza Virus Neuraminidase Detection and Purification.Angewandte Chemie (International ed. in English) · 2025Article
- Identification of a seasonal influenza vaccine-induced broadly protective neuraminidase antibody.The Journal of experimental medicine · 2025Article
- DNA and protein-generated chimeric molecules for delivery of influenza viral epitopes in mouse and humanized NSG transfer models.Human vaccines & immunotherapeutics · 2024Review
- Development and characterization of an antibody that recognizes influenza virus N1 neuraminidases.PloS one · 2024Article
- Human anti-N1 monoclonal antibodies elicited by pandemic H1N1 virus infection broadly inhibit HxN1 viruses in vitro and in vivo.Immunity · 2023Article
- A broadly protective human monoclonal antibody targeting the sialidase activity of influenza A and B virus neuraminidases.Nature communications · 2022Article
- Antigenic characterization of influenza and SARS-CoV-2 viruses.Analytical and bioanalytical chemistry · 2022Review
- Article
- Antivirals Targeting the Neuraminidase.Cold Spring Harbor perspectives in medicine · 2022Review
- Antibodies directed towards neuraminidase restrict influenza virus replication in primary human bronchial epithelial cells.PloS one · 2022Article
- Avian influenza A (H7N9) virus: from low pathogenic to highly pathogenic.Frontiers of medicine · 2021Review
- Flu Universal Vaccines: New Tricks on an Old Virus.Virologica Sinica · 2021Review
- Influenza Neuraminidase Characteristics and Potential as a Vaccine Target.Frontiers in immunology · 2021Review
- Novel pathogenic characteristics of highly pathogenic avian influenza virus H7N9: viraemia and extrapulmonary infection.Emerging microbes & infections · 2020Article
- Article
- Generation of neutralizing and non-neutralizing monoclonal antibodies against H7N9 influenza virus.Emerging microbes & infections · 2020Article
- Protective efficacy of anti-neuraminidase monoclonal antibodies against H7N9 influenza virus infection.Emerging microbes & infections · 2020Article
- Influenza H7N9 Virus Neuraminidase-Specific Human Monoclonal Antibodies Inhibit Viral Egress and Protect from Lethal Influenza Infection in Mice.Cell host & microbe · 2019Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
Zoonotic A(H7N9) avian influenza viruses emerged in China in 2013 and continue to be a threat to human public health, having infected over 800 individuals with a mortality rate approaching 40%. Treatment options for people infected with A(H7N9) include the use of neuraminidase (NA) inhibitors. However, like other influenza viruses, A(H7N9) can become resistant to these drugs. The use of monoclonal antibodies is a rapidly developing strategy for controlling influenza virus infection. Here we generated a murine monoclonal antibody (3c10-3) directed against the NA of A(H7N9) and show that prophylactic systemic administration of 3c10-3 fully protected mice from lethal challenge with wild-type A/Anhui/1/2013 (H7N9). Further, post-infection treatment with a single systemic dose of 3c10-3 at either 24, 48 or 72 h post A(H7N9) challenge resulted in both dose- and time-dependent protection of up to 100% of mice, demonstrating therapeutic potential for 3c10-3. Epitope mapping revealed that 3c10-3 binds near the enzyme active site of NA, and functional characterization showed that 3c10-3 inhibits the enzyme activity of NA and restricts the cell-to-cell spread of the virus in cultured cells. Affinity analysis also revealed that 3c10-3 binds equally well to recombinant NA of wild-type A/Anhui/1/2013 and to a variant NA carrying a R289K mutation known to infer NAI resistance. These results suggest that 3c10-3 has the potential to be used as a therapeutic to treat A(H7N9) infections either as an alternative to, or in combination with, current NA antiviral inhibitors.
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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.