In one paragraphArticle in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from itWhat 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.
2 · The registryThe 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.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
18 authors.
Katherine MarougkaSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0000-0002-1807-5751 Rocío Leiva-RebolloDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.ORCID 0000-0001-9407-8084 Freeke HofmaSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0009-0005-0822-4281 Albert van DijkComplex Cell Culture Facility, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0000-0002-8664-3730 Nancy N M P SchuurmanSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.
Shervin KaandorpSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0009-0005-6182-3355 Xuesheng WuSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0000-0001-8136-1446 Mengying LiuSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.
Louisa E WallaceSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0000-0002-6210-8645 Lemeng ChaoChemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht 3584 CG, The Netherlands.
Tom WennekesChemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht 3584 CG, The Netherlands.ORCID 0000-0002-2368-7728 Elif UsluChemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht 3584 CG, The Netherlands.ORCID 0009-0009-3678-1893 Geert-Jan BoonsChemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht 3584 CG, The Netherlands.ORCID 0000-0003-3111-5954 Loes A den Hertog-OosterhoffLab of Cellular Disease Models, Department of Pediatrics, Regenerative Medicine Center Utrecht, University Medical Center Utrecht, Utrecht 3584 CT, The Netherlands.
Gimano D AmatngalimLab of Cellular Disease Models, Department of Pediatrics, Regenerative Medicine Center Utrecht, University Medical Center Utrecht, Utrecht 3584 CT, The Netherlands.ORCID 0000-0003-3442-1754 Erik de VriesSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.
Adolfo García-SastreDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029.ORCID 0000-0002-6551-1827 Cornelis A M de HaanSection Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht 3584 CL, The Netherlands.ORCID 0000-0002-4459-9874 Funding
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) 75N93021R00014ZonMw (Netherlands Organisation for Health Research and Development) 10710022210003
6 · The paper itselfAbstract
Swine are a crucial species in influenza A virus (IAV) ecology, capable of supporting replication and consequently evolution of human, avian, and swine strains. They are also the source of the 2009 pandemic H1N1 virus (H1N1pdm09). Understanding how swine IAV breach the species barrier is essential for detection of potentially pandemic viruses, but is often overlooked compared to avian IAV. We hypothesize that the HA-NA balance of (pre)pandemic swine viruses is a key feature that needs adjustment as swine and humans differ in their sialoglycome. We focused on a set of (pre)pandemic swine viruses collected in Mexico following the H1N1pdm09 emergence. Phylogenetic analysis showed that the emergence was preceded by substitutions in HA and NA predicted to affect their function. Thus, HA acquired substitution A227E, previously shown to reduce receptor binding in H1N1pdm09, while NA obtained substitution S369N in the 2nd sialic acid binding site (2SBS) predicted to reduce NA cleavage. The substitutions' effect on the HA-NA balance, was confirmed with biolayer interferometry using recombinant proteins attached to nanoparticles. Engineering recombinant attenuated influenza viruses with swine HA and NA with/without the mentioned substitutions, showed that the 2SBS substitution negatively affected replication in primary human and swine cultures. Interestingly, replication was restored by the HA substitution. Overall, we show that the emergence of H1N1pdm09 in humans was preceded by substitutions in HA and NA that were acquired in swine and adjusted the HA-NA balance. We hypothesize that adjustment of the HA-NA balance was a critical step for crossing the host-species barrier.
Indexed as
Hemagglutinin Glycoproteins, Influenza VirusInfluenza A Virus, H1N1 SubtypeInfluenza, HumanNeuraminidaseOrthomyxoviridae InfectionsReceptors, VirusViral ProteinsAmino Acid SubstitutionAnimalsDogsHumansMexicoPandemicsPhylogenySwineVirus ReplicationHemagglutinin Glycoproteins, Influenza VirusNA protein, influenza A virusNeuraminidaseReceptors, VirusViral ProteinsHA–NA balanceinfluenza A viruspandemicreceptor bindingreceptor cleaving
Identifiers
PMID42776754
PMCPMC13624637
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