ArticleScientific reports2017
Adaptation of influenza A (H7N9) virus in primary human airway epithelial cells.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.
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Who cites it
13 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.
- Pooled it
- Comparative Immunogenicity of Inactivated H7N9 Avian Influenza Vaccines with Different Internal Gene Backbones.Microorganisms · 2026Article
- Article
- Article
- The convergent evolution of influenza A virus: Implications, therapeutic strategies and what we need to know.Current research in microbial sciences · 2023Article
- H7N9 Influenza Virus in China.Cold Spring Harbor perspectives in medicine · 2021Review
- Tradeoffs for a viral mutant with enhanced replication speed.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Evolution and Adaptation of the Avian H7N9 Virus into the Human Host.Microorganisms · 2020Review
- Hypertension, Thrombosis, Kidney Failure, and Diabetes: Is COVID-19 an Endothelial Disease? A Comprehensive Evaluation of Clinical and Basic Evidence.Journal of clinical medicine · 2020Review
- COVID-19 and the endothelium.Clinical hemorheology and microcirculation · 2020Article
- The Importance of Vaccinating Children and Pregnant Women against Influenza Virus Infection.Pathogens (Basel, Switzerland) · 2019Review
- Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A (H7N9) is an emerging zoonotic pathogen with pandemic potential. To understand its adaptation capability, we examined the genetic changes and cellular responses following serial infections of A (H7N9) in primary human airway epithelial cells (hAECs). After 35 serial passages, six amino acid mutations were found, i.e. HA (R54G, T160A, Q226L, H3 numbering), NA (K289R, or K292R for N2 numbering), NP (V363V/I) and PB2 (L/R332R). The mutations in HA enabled A(H7N9) virus to bind with higher affinity (from 39.2% to 53.4%) to sialic acid α2,6-galactose (SAα2,6-Gal) linked receptors. A greater production of proinflammatory cytokines in hAECs was elicited at later passages together with earlier peaking at 24 hours post infection of IL-6, MIP-1α, and MCP-1 levels. Viral replication capacity in hAECs maintained at similar levels throughout the 35 passages. In conclusion, during the serial infections of hAECs by influenza A(H7N9) virus, enhanced binding of virion to cell receptors with subsequent stronger innate cell response were noted, but no enhancement of viral replication could be observed. This indicates the existence of possible evolutional hurdle for influenza A(H7N9) virus to transmit efficiently from human to human.
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