Drift and shape—new insights into human immunity against influenza virus neuraminidase
ABSTRACTInfluenza virus hemagglutinin mediates infection by binding sialic acids, whereas neuraminidase cleaves sialic acids to release progeny virions. Both are targets of protective antibodies, but influenza vaccine strain selection and antigen dose are based on hemagglutinin alone. Virus characte...
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| Format: | Article |
| Language: | English |
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American Society for Microbiology
2023-12-01
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| Series: | mBio |
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| Online Access: | https://journals.asm.org/doi/10.1128/mbio.01654-23 |
| _version_ | 1797378888625553408 |
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| author | Annette Fox |
| author_facet | Annette Fox |
| author_sort | Annette Fox |
| collection | DOAJ |
| description | ABSTRACTInfluenza virus hemagglutinin mediates infection by binding sialic acids, whereas neuraminidase cleaves sialic acids to release progeny virions. Both are targets of protective antibodies, but influenza vaccine strain selection and antigen dose are based on hemagglutinin alone. Virus characterization using first infection ferret sera indicates that escape from hemagglutination inhibiting (HI) antibodies occurs more frequently and is not coordinated with escape from neuraminidase inhibiting (NI) antibodies. A key question addressed by Daulagala et al. (P. Daulagala, B. R. Mann, K. Leung, E. H. Y. Lau, et al., mBio 14:e00084-23, 2023, https://doi.org/10.1128/mbio.00084-23) is how this translates to humans who encounter multiple influenza viruses throughout life. Their cross-sectional study, using sera from a wide age range of participants and H1N1 viruses spanning 1977–2015, indicates that NI antibodies are more broadly cross-reactive than HI antibodies. Both HI and NI titers were highest against strains encountered in childhood indicating that both are shaped by priming exposures. The study further supports the development of NA-optimized vaccines. |
| first_indexed | 2024-03-08T20:14:08Z |
| format | Article |
| id | doaj.art-82a25d08991c4ca59a6f790732abb584 |
| institution | Directory Open Access Journal |
| issn | 2150-7511 |
| language | English |
| last_indexed | 2024-03-08T20:14:08Z |
| publishDate | 2023-12-01 |
| publisher | American Society for Microbiology |
| record_format | Article |
| series | mBio |
| spelling | doaj.art-82a25d08991c4ca59a6f790732abb5842023-12-22T19:53:44ZengAmerican Society for MicrobiologymBio2150-75112023-12-0114610.1128/mbio.01654-23Drift and shape—new insights into human immunity against influenza virus neuraminidaseAnnette Fox0WHO Collaborating Centre for Reference and Research on Influenza, Royal Melbourne Hospital, at the Peter Doherty Institute for Infection and Immunity, Melbourne, Victoria, AustraliaABSTRACTInfluenza virus hemagglutinin mediates infection by binding sialic acids, whereas neuraminidase cleaves sialic acids to release progeny virions. Both are targets of protective antibodies, but influenza vaccine strain selection and antigen dose are based on hemagglutinin alone. Virus characterization using first infection ferret sera indicates that escape from hemagglutination inhibiting (HI) antibodies occurs more frequently and is not coordinated with escape from neuraminidase inhibiting (NI) antibodies. A key question addressed by Daulagala et al. (P. Daulagala, B. R. Mann, K. Leung, E. H. Y. Lau, et al., mBio 14:e00084-23, 2023, https://doi.org/10.1128/mbio.00084-23) is how this translates to humans who encounter multiple influenza viruses throughout life. Their cross-sectional study, using sera from a wide age range of participants and H1N1 viruses spanning 1977–2015, indicates that NI antibodies are more broadly cross-reactive than HI antibodies. Both HI and NI titers were highest against strains encountered in childhood indicating that both are shaped by priming exposures. The study further supports the development of NA-optimized vaccines.https://journals.asm.org/doi/10.1128/mbio.01654-23influenzahumoral immunityimmune memoryneuraminidaseantigenic variation |
| spellingShingle | Annette Fox Drift and shape—new insights into human immunity against influenza virus neuraminidase mBio influenza humoral immunity immune memory neuraminidase antigenic variation |
| title | Drift and shape—new insights into human immunity against influenza virus neuraminidase |
| title_full | Drift and shape—new insights into human immunity against influenza virus neuraminidase |
| title_fullStr | Drift and shape—new insights into human immunity against influenza virus neuraminidase |
| title_full_unstemmed | Drift and shape—new insights into human immunity against influenza virus neuraminidase |
| title_short | Drift and shape—new insights into human immunity against influenza virus neuraminidase |
| title_sort | drift and shape new insights into human immunity against influenza virus neuraminidase |
| topic | influenza humoral immunity immune memory neuraminidase antigenic variation |
| url | https://journals.asm.org/doi/10.1128/mbio.01654-23 |
| work_keys_str_mv | AT annettefox driftandshapenewinsightsintohumanimmunityagainstinfluenzavirusneuraminidase |