Changes in the hemagglutinin of H5N1 viruses during human infection--influence on receptor binding.

Martin Crusat1,2 Junfeng Liu Angelina S Palma Robert A Childs Yan Liu Stephen A Wharton Yi Pu Lin Peter J Coombs Stephen R Martin Mikhail Matrosovich Zi Chen David J Stevens Vo Minh Hien Tran Tan Thanh Le Nguyen Truc Nhu Lam Anh Nguyet Do Quang Ha H Rogier van Doorn Tran Tinh Hien Harald S Conradt Makoto Kiso Steve J Gamblin Wengang Chai John J Skehel Alan J Hay Jeremy Farrar Menno D de Jong Ten Feizi
Affiliations 2 institutions
  1. Oxford University Clinical Research Unit, Hospital for Tropical Diseases, Ho Chi Minh City, Vietnam
  2. Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
Active Last checked 2026-10-08 03:30:35 Source: NCBI PubMed

Abstract

As avian influenza A(H5N1) viruses continue to circulate in Asia and Africa, global concerns of an imminent pandemic persist. Recent experimental studies suggest that efficient transmission between humans of current H5N1 viruses only requires a few genetic changes. An essential step is alteration of the virus hemagglutinin from preferential binding to avian receptors for the recognition of human receptors present in the upper airway. We have identified receptor-binding changes which emerged during H5N1 infection of humans, due to single amino acid substitutions, Ala134Val and Ile151Phe, in the hemagglutinin. Detailed biological, receptor-binding, and structural analyses revealed reduced binding of the mutated viruses to avian-like receptors, but without commensurate increased binding to the human-like receptors investigated, possibly reflecting a receptor-binding phenotype intermediate in adaptation to more human-like characteristics. These observations emphasize that evolution in nature of avian H5N1 viruses to efficient binding of human receptors is a complex multistep process.

Supporting text Virus Host Location
Biolayer interferometry 2 Carbohydrate microarray 1 H5N1 influenza infection 1 Hemagglutination assays 1 Hemagglutinin 32 Hemagglutinin X-ray crystal structure 1 Pyrosequencing 1 Receptor binding 33 Receptor specificity 4 Synthetic sialylglycopolymers 1 Mutation, Missense 26 Virus Attachment 55 Animals 1981 Crystallography, X-Ray 32 Hemagglutinin Glycoproteins, Influenza Virus 183 Humans 1455 Influenza A Virus, H5N1 Subtype 308 Influenza in Birds 352 Influenza, Human 290 Mutant Proteins 15 Poultry 115 Protein Binding 194 Protein Conformation 44 Receptors, Virus 208

Evidence records

1 total
Functional Mechanism
1 records · 1 evidence types
Evidence type
1 records
OVE1573
Key finding

Ala134Val and Ile151Phe substitutions in the hemagglutinin of H5N1 viruses emerged during human infection and modified receptor-binding toward an intermediate phenotype between avian- and human-type receptors.

Virus
Host
Not specified
Location
Not specified
Supporting text

We have identified receptor-binding changes which emerged during H5N1 infection of humans, due to single amino acid substitutions, Ala134Val and Ile151Phe, in the hemagglutinin.

Genes or proteins
hemagglutinin
Receptors
avian-like receptors | human-like receptors
Mutations
Ala134Val | Ile151Phe
Mechanism types
receptor binding | host-range expansion