ArticleEmerging microbes & infections2026
HA Protein acetylation modulates replication, pathogenicity, and immunogenicity of influenza virus and facilitates live-attenuated vaccine design.
Article in Emerging microbes & infections, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Post-translational modification networks as master regulators of influenza virus replication, host adaptation, and immune evasion.Frontiers in immunology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysine acetylation, a form of protein post-translational modification (PTM), is known to play crucial roles in regulating cellular and physiological processes. In this study, for the first time, lysine acetylation sites were identified on the hemagglutinin (HA) protein of H1N1 subtype influenza virus using mass spectrometry analysis, including K157, K169, K418, and K459. To elucidate the functional significance of these acetylation sites, eight mutant viruses featuring arginine substitutions (K157R, K169R, K418R, or K459R) to mimic deacetylated states and glutamine substitutions (K157Q, K169Q, K418Q, or K459Q) to mimic constitutively acetylated states were generated by reverse genetics. In mouse model, deacetylation mutants exhibited significantly attenuated virulence compared to wild-type. Interestingly, while the acetylation-mimetic K157Q and K418Q restored viral virulence, the K169Q and K459Q mutants failed to restore the pathogenicity. These findings suggest that acetylation at K157 and K418 and dynamical acetylation at residues K169 and K459 are essential for the virulence of influenza virus. Subsequent investigations revealed that acetylation plays a pivotal role in the pH stability of HA protein, mediating viral pathogenicity. Given the critical role of HA acetylation in viral virulence, we investigated the potential of avirulent viruses K157R, K169Q, or K418R as promising live-attenuated vaccine candidates. Notably, the K418R mutant, which caused no detectable weight loss, was particularly safe and provided full protection against wild-type influenza virus challenge in mouse model. This study highlights the critical role of HA acetylation modification in influenza virus pathogenicity and offers a new strategy for the development of influenza virus vaccine.
Indexed as
Identifiers
What OpenQuestion holds
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.