Changes in the hemagglutinin of H5N1 viruses during human infection - Influence on receptor binding
| Autor: | Steve J. Gamblin, Stephen R. Martin, Junfeng Liu, P.J. Coombs, Vo Minh Hien, Tran Tinh Hien, Tran Tan Thanh, Jeremy Farrar, H. Rogier van Doorn, Ten Feizi, D.J. Stevens, Lam Anh Nguyet, Mikhail Matrosovich, Harald S. Conradt, Angelina S. Palma, Yan Liu, Robert A. Childs, Zi-Qiang Chen, Le Nguyen Truc Nhu, Alan J. Hay, Yi Pu Lin, Wengang Chai, Martin Crusat, Stephen A. Wharton, John J. Skehel, Menno D. de Jong, Makoto Kiso, Do Quang Ha |
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| Přispěvatelé: | Other departments, Medical Microbiology and Infection Prevention, Amsterdam institute for Infection and Immunity |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
H5N1 influenza infection
Biolayer interferometry Protein Conformation Hemagglutinin Glycoproteins Influenza Virus Plasma protein binding Acoplamiento Viral Crystallography X-Ray medicine.disease_cause Poultry Protein structure Mutación Missense Hemagglutinin Receptor 0303 health sciences biology Pyrosequencing Hemagglutinin X-ray crystal structure Phenotype 3. Good health Receptor specificity Synthetic sialylglycopolymers RNA Viral Receptors Virus Protein Binding Viral protein Mutation Missense Virus Attachment Hemagglutinin (influenza) Proteínas Mutantes Article Virus 03 medical and health sciences Virology Influenza Human medicine Animals Humans Hemagglutination assays 030304 developmental biology Carbohydrate microarray Influenza A Virus H5N1 Subtype 030306 microbiology Gripe Aviar Sequence Analysis DNA Cristalografía por Rayos X Glicoproteínas Hemaglutininas del Virus de la Influenza Subtipo H5N1 del Virus de la Influenza A Influenza A virus subtype H5N1 Influenza in Birds biology.protein Receptor binding Mutant Proteins |
| Zdroj: | RUNA. Repositorio da Consellería de Sanidade e Sergas Servizo Galego de Saúde (SERGAS) Virology, 447(1-2), 326-337. Academic Press Inc. Virology |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2013.08.010 |
| Popis: | 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. Highlights • Changes in receptor binding of HA during H5N1 human infection were identified. • Single A134V and L151F substitutions caused reduced affinity for avian receptors. • Glycan array analyses were used to identify changes in receptor binding specificity. • Structural basis for altered receptor binding was examined by X-ray crystallography. |
| Databáze: | OpenAIRE |
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