Article

Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations

2026-04-16

Abstract excerpt

It has been suggested that the hemagglutinin of the human-infecting cattle-derived 2.3.4.4b virus A/Texas/34 (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 tha...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: e0a5b71e-16e1-59a8-8d4e-f525b97e3e2e
DOI: 10.64898/2026.04.16.718875

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutationsDOI 10.64898/2026.04.16.718875Read

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptorsSemantic proximity Read

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptorsSemantic proximity Read

A single mutation in dairy cow-associated H5N1 viruses increases receptor binding breadthSemantic proximity Read

The Q226H Mutation in Avian H5N1 Hemagglutinin Mediates a Path towards Structural Adaptation in HumansSemantic proximity Read

A single mutation in Taiwanese H6N1 influenza hemagglutinin switches binding to human‐type receptorsSemantic proximity Read

A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors.Semantic proximity Read

Genetic determinants of receptor-binding preference and zoonotic potential of H9N2 avian influenza virusesSemantic proximity Read

Changes in the hemagglutinin of H5N1 viruses during human infection – Influence on receptor bindingSemantic proximity Read

Structural determinants for naturally evolving H5N1 hemagglutinin to switch its receptor specificity.Semantic proximity Read

Structural Basis for a Switch in Receptor Binding Specificity of Two H5N1 Hemagglutinin Mutants.Semantic proximity Read

Hemagglutinin double-mutation enhances binding of human-infecting avian influenza virus clade 2.3.4.4b H5Ny to human and SLeX receptors.Semantic proximity Read

What adaptive changes in hemagglutinin and neuraminidase are necessary for emergence of pandemic influenza virus from its avian precursor?Semantic proximity Read