ArticleJournal of visualized experiments : JoVE2013
Expression of functional recombinant hemagglutinin and neuraminidase proteins from the novel H7N9 influenza virus using the baculovirus expression system.
Article in Journal of visualized experiments : JoVE, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 165 papers.
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Who cites it
165 citing papers in PubMed, 181 citations in OpenAlex.
- Assessing the Protective Potential of H1N1 Influenza Virus Hemagglutinin Head and Stalk Antibodies in Humans.Journal of virology · 2019Trial
- Pre-existing hemagglutinin-specific antibody levels are associated with B-cell repertoire maturation and antibody breadth after influenza vaccination.Virologica Sinica · 2026Article
- Beyond the blood: Tissue-resident immunity shapes SARS-CoV-2 vaccine antibody responses.bioRxiv : the preprint server for biology · 2026Article
- Hemagglutination Inhibition and Alternate Serologic Responses Following Influenza A(H3N2) Virus Infection.Influenza and other respiratory viruses · 2026Article
- Influenza B mosaic HA mRNA-LNP vaccines are cross-reactive and protective in mice.Molecular therapy. Nucleic acids · 2026Article
- Population immunity to clade 2.3.4.4b H5N1 is dominated by anti-neuraminidase antibodies.mBio · 2026Article
- A TRAC-478-adjuvanted recombinant N1 neuraminidase influenza virus vaccine induces balanced and broadly protective immune responses.NPJ vaccines · 2026Article
- Hemagglutination inhibition and alternate serologic responses following Influenza A(H3N2) virus infection.medRxiv : the preprint server for health sciences · 2026Article
- Encapsulation of the lipidated TLR7/8 agonist INI-4001 into ionic liposomes impacts H7 influenza antigen-specific immune responses.Drug delivery and translational research · 2026Article
- Structural and functional characterization of the antigenicity of influenza A virus hemagglutinin subtype H15.Cell reports · 2026Article
- 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
- Adjuvanted influenza vaccination increases pre-existing H5N1 cross-reactive antibodies.Nature communications · 2026Article
- Distinct components of mRNA vaccines cooperate to instruct efficient germinal center responses.Cell · 2025Article
- Human monoclonal antibodies that target clade 2.3.4.4b H5N1 hemagglutinin.Nature communications · 2025Article
- Anti-neuraminidase and anti-HA stalk antibodies reduce the susceptibility to and infectivity of influenza A/H3N2 virus.Nature communications · 2025Article
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- The hemagglutinin proteins of clades 1 and 2.3.4.4b H5N1 highly pathogenic avian influenza viruses exhibit comparable attachment patterns to avian and mammalian tissues.Journal of virology · 2025Article
- Assessment of critical bioprocess parameters for broadly cross-reactive chimeric hemagglutinin influenza virus vaccines.Vaccine · 2025Article
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105 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The baculovirus expression system is a powerful tool for expression of recombinant proteins. Here we use it to produce correctly folded and glycosylated versions of the influenza A virus surface glycoproteins - the hemagglutinin (HA) and the neuraminidase (NA). As an example, we chose the HA and NA proteins expressed by the novel H7N9 virus that recently emerged in China. However the protocol can be easily adapted for HA and NA proteins expressed by any other influenza A and B virus strains. Recombinant HA (rHA) and NA (rNA) proteins are important reagents for immunological assays such as ELISPOT and ELISA, and are also in wide use for vaccine standardization, antibody discovery, isolation and characterization. Furthermore, recombinant NA molecules can be used to screen for small molecule inhibitors and are useful for characterization of the enzymatic function of the NA, as well as its sensitivity to antivirals. Recombinant HA proteins are also being tested as experimental vaccines in animal models, and a vaccine based on recombinant HA was recently licensed by the FDA for use in humans. The method we describe here to produce these molecules is straight forward and can facilitate research in influenza laboratories, since it allows for production of large amounts of proteins fast and at a low cost. Although here we focus on influenza virus surface glycoproteins, this method can also be used to produce other viral and cellular surface proteins.
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