---
title: "Multiple mutations, not Q226L alone, enable 2.3.4.4b H5N1 hemagglutinins to bind human respiratory"
id: "pubmed-42573239"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42573239"
content_type: "clinical_feed_article"
specialty: "Critical Care"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42573239/"
doi: "10.1128/jvi.01065-26"
published_at: "2026-09-22T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Multiple mutations, not Q226L alone, enable 2.3.4.4b H5N1 hemagglutinins to bind human respiratory
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42573239
- **Specialty:** [Critical Care](https://medichelpline.com/clinical-feed/critical-care.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42573239/)
- **DOI:** [10.1128/jvi.01065-26](https://doi.org/10.1128%2Fjvi.01065-26)
- **Published At:** 2026-09-22T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- The study evaluated receptor binding of hemagglutinins from **2.3.4.4b H5N1** lineage viruses, focusing on the Q226L substitution and additional mutations. - Researchers tested binding of H5TX Q226L (from A/Texas/34 H5N1) and other mutants to sections of the **human trachea** rather than relying solely on synthetic glycans. - The H5TX Q226L mutant can bind **human-type receptors** in glycan assays, but tissue-based assays showed that **a single Q226L mutation is insufficient** for binding human respiratory tract tissue. - An H5FR Q226L mutant (from A/duck/France/161108/16 H5N8) exhibited altered receptor-binding specificity; this change was associated with the presence of a **multibasic cleavage site**. - The data indicate that acquisition of human-type receptor binding in currently circulating H5Nx viruses likely requires **multiple amino acid substitutions** and may be influenced by additional HA features such as cleavage site motifs. - The authors emphasize the importance of testing individual strains with complementary methods, including **tissue-based approaches**, alongside synthetic glycan analyses to assess human adaptation potential. - The work provides insight into determinants of evolution toward human-type receptor binding but does not report human-to-human transmission; it frames findings in the context of zoonotic spillover events and host range expansion. - Keywords highlighted in the study include: **2.3.4.4b H5N1**, N-glycan, **hemagglutinin**, influenza, receptor binding, and sialic acid.
## Clinical Analysis & Structured Key Points
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Epub 2026 Aug 10. # Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations [María Ríos Carrasco](https://pubmed.ncbi.nlm.nih.gov/?term=R%C3%ADos+Carrasco+M&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Mafalda F Guerreiro Cabana](https://pubmed.ncbi.nlm.nih.gov/?term=Guerreiro+Cabana+MF&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Eszter Kovács](https://pubmed.ncbi.nlm.nih.gov/?term=Kov%C3%A1cs+E&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Zoé Ducarne](https://pubmed.ncbi.nlm.nih.gov/?term=Ducarne+Z&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Cindy G J Cleypool](https://pubmed.ncbi.nlm.nih.gov/?term=Cleypool+CGJ&cauthor_id=42573239)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-2 "Division of Surgical Specialties, Department of Anatomy, University Medical Center Utrecht, Utrecht University, Utrecht, the Netherlands."), [Geert-Jan Boons](https://pubmed.ncbi.nlm.nih.gov/?term=Boons+G-J&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.")[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-3 "Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA."), [Robert P de Vries](https://pubmed.ncbi.nlm.nih.gov/?term=de+Vries+RP&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#full-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.") Affiliations Expand ### Affiliations * 1 Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands. * 2 Division of Surgical Specialties, Department of Anatomy, University Medical Center Utrecht, Utrecht University, Utrecht, the Netherlands. * 3 Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA. * PMID: **42573239** * DOI: [ 10.1128/jvi.01065-26 ](https://doi.org/10.1128/jvi.01065-26) Item in Clipboard # Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations María Ríos Carrasco et al. J Virol. 2026. Show details Display options Display options Format Abstract PubMed PMID J Virol Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22J+Virol%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22J+Virol%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42573239/) . 2026 Sep 22;100(9):e0106526. doi: 10.1128/jvi.01065-26. Epub 2026 Aug 10. ### Authors [María Ríos Carrasco](https://pubmed.ncbi.nlm.nih.gov/?term=R%C3%ADos+Carrasco+M&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Mafalda F Guerreiro Cabana](https://pubmed.ncbi.nlm.nih.gov/?term=Guerreiro+Cabana+MF&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Eszter Kovács](https://pubmed.ncbi.nlm.nih.gov/?term=Kov%C3%A1cs+E&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Zoé Ducarne](https://pubmed.ncbi.nlm.nih.gov/?term=Ducarne+Z&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands."), [Cindy G J Cleypool](https://pubmed.ncbi.nlm.nih.gov/?term=Cleypool+CGJ&cauthor_id=42573239)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-2 "Division of Surgical Specialties, Department of Anatomy, University Medical Center Utrecht, Utrecht University, Utrecht, the Netherlands."), [Geert-Jan Boons](https://pubmed.ncbi.nlm.nih.gov/?term=Boons+G-J&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.")[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-3 "Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA."), [Robert P de Vries](https://pubmed.ncbi.nlm.nih.gov/?term=de+Vries+RP&cauthor_id=42573239)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42573239/#short-view-affiliation-1 "Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands.") ### Affiliations * 1 Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, the Netherlands. * 2 Division of Surgical Specialties, Department of Anatomy, University Medical Center Utrecht, Utrecht University, Utrecht, the Netherlands. * 3 Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA. * PMID: **42573239** * DOI: [ 10.1128/jvi.01065-26 ](https://doi.org/10.1128/jvi.01065-26) Item in Clipboard Full text links Cite Display options Display options Format Abstract PubMed PMID ## Abstract It has been suggested that the hemagglutinin of the human-infecting cattle-derived 2.3.4.4b virus A/Texas/34 H5N1 (H5TX) requires only one mutation, namely Q226L, to switch from binding avian-type to human-type receptor preference. In this study, we examined the binding of H5TX Q226L, along with other key mutations, to sections of human trachea. We conclude that, while H5TX Q226L can bind human-type receptors, more than a single mutation is required for this protein to bind to human respiratory tract tissue. We also report changes in receptor-binding specificity of another 2.3.4.4b HA mutant, H5FR Q226L (from A/duck/France/161108/16 H5N8), associated with the presence of a multibasic cleavage site. This study offers insight into the determinants of evolution toward human-type receptor binding in currently circulating H5Nx viruses. It also emphasizes the importance of testing individual strains using additional methods, including tissue-based approaches, alongside synthetic glycans.IMPORTANCECurrently, H5N1 influenza A viruses are responsible for numerous zoonotic spillover events, from infecting birds to other mammals, including dairy cattle. Although no human-to-human transmission has been observed, several people have been infected. This host range expansion is typically linked to changes in one of the viral surface proteins, hemagglutinin, which can switch its preference from avian-type to human-type receptors. To better understand the potential of the currently circulating H5N1 virus to transmit among humans, we evaluated the effects of the Q226L mutation, in combination with other amino acid substitutions, on binding to the human trachea. We also studied the effect of the multibasic cleavage site, a specific motif present in highly pathogenic influenza strains, on receptor-binding properties. These findings provide insight into the role of receptor binding in influenza infections. **Keywords:** 2.3.4.4b H5N1; N-glycan; hemagglutinin; influenza; receptor binding; sialic acid. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## Conflict of interest statement The authors declare no conflict of interest. ## Similar articles * [ 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. ](https://pubmed.ncbi.nlm.nih.gov/40985723/) Zhu B, Fung K, Feng HH, Beatty JA, Hill F, Tse ACN, Brackman CJ, Sit THC, Poujade A, Gaide N, Ducatez M, Foucras G, Peiris M, Ti S-C, Nicholls JM, Yen H-L.Zhu B, et al.J Virol. 2025 Oct 23;99(10):e0097625. doi: 10.1128/jvi.00976-25. Epub 2025 Sep 23.J Virol. 2025.PMID: 40985723Free PMC article. * [ Enhanced Human-Type Receptor Binding by Ferret-Transmissible H5N1 with a K193T Mutation. ](https://pubmed.ncbi.nlm.nih.gov/29491160/) Peng W, Bouwman KM, McBride R, Grant OC, Woods RJ, Verheije MH, Paulson JC, de Vries RP.Peng W, et al.J Virol. 2018 Apr 27;92(10):e02016-17. doi: 10.1128/JVI.02016-17. Print 2018 May 15.J Virol. 2018.PMID: 29491160Free PMC article. * [ The bovine mammary gland as a crucible for zoonotic influenza virus emergence: Receptor-mediated adaptation of HPAI H5N1 clade 2.3.4.4b. ](https://pubmed.ncbi.nlm.nih.gov/41723792/) Naveed A.Naveed A.Arch Virol. 2026 Feb 22;171(3):89. doi: 10.1007/s00705-026-06529-0.Arch Virol. 2026.PMID: 41723792Review. * [ Decoding non-human mammalian adaptive signatures of 2.3.4.4b H5N1 to assess its human adaptive potential. ](https://pubmed.ncbi.nlm.nih.gov/40788041/) Nataraj R, Ashok AK, Dey AA, Kesavardhana S.Nataraj R, et al.Microbiol Spectr. 2025 Sep 2;13(9):e0094825. doi: 10.1128/spectrum.00948-25. Epub 2025 Aug 11.Microbiol Spectr. 2025.PMID: 40788041Free PMC article. * [ Avian influenza A (H5N1) virus in dairy cattle: origin, evolution, and cross-species transmission. ](https://pubmed.ncbi.nlm.nih.gov/39535188/) Mostafa A, Naguib MM, Nogales A, Barre RS, Stewart JP, García-Sastre A, Martinez-Sobrido L.Mostafa A, et al.mBio. 2024 Dec 11;15(12):e0254224. doi: 10.1128/mbio.02542-24. Epub 2024 Nov 13.mBio. 2024.PMID: 39535188Free PMC article.Review. 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