Highly Pathogenic Influenza A(H5Nx) Viruses with Altered H5 Receptor-Binding Specificity
| Autor: | Guo, Hongbo, de Vries, Erik, McBride, Ryan, Dekkers, Jojanneke, Bouwman, Kim M, Nycholat, Corwin, Verheije, M Helene, Paulson, James C, van Kuppeveld, Frank J M, de Haan, Cornelis A M, dI&I I&I-1, LS Virologie, LS Pathologie, dIRAS RA-1, dPB I&I |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Epidemiology receptor binding lcsh:Medicine highly pathogenic Hemagglutinin Glycoproteins Influenza Virus medicine.disease_cause phylogeny Influenza A virus H5Nx virus fucosylated sialosides biology 3. Good health Infectious Diseases Ducks Receptors Virus influenza Reassortant Viruses Microbiology (medical) Genotype 030106 microbiology Hemagglutinin (influenza) Virus Attachment H5N1 genetic structure Virus Antigenic drift lcsh:Infectious and parasitic diseases 03 medical and health sciences Structure-Activity Relationship H5 protein Influenza Human medicine H5Nx subtype virus Animals Humans influenza A virus emergence lcsh:RC109-216 viruses hemagglutinin Alleles Research lcsh:R Virology Influenza A virus subtype H5N1 Viral Tropism 030104 developmental biology Amino Acid Substitution Highly Pathogenic Influenza A(H5Nx) Viruses with Altered H5 Receptor-Binding Specificity Influenza in Birds Mutation biology.protein Tissue tropism virus clade 2.3.4.4 |
| Zdroj: | Emerging Infectious Diseases Emerging Infectious Diseases, 23(2). Centers for Disease Control and Prevention (CDC) Emerging Infectious Diseases, Vol 23, Iss 2, Pp 220-231 (2017) |
| ISSN: | 1080-6059 1080-6040 |
| Popis: | Emergence and intercontinental spread of highly pathogenic avian influenza A(H5Nx) virus clade 2.3.4.4 is unprecedented. H5N8 and H5N2 viruses have caused major economic losses in the poultry industry in Europe and North America, and lethal human infections with H5N6 virus have occurred in Asia. Knowledge of the evolution of receptor-binding specificity of these viruses, which might affect host range, is urgently needed. We report that emergence of these viruses is accompanied by a change in receptor-binding specificity. In contrast to ancestral clade 2.3.4 H5 proteins, novel clade 2.3.4.4 H5 proteins bind to fucosylated sialosides because of substitutions K222Q and S227R, which are unique for highly pathogenic influenza virus H5 proteins. North American clade 2.3.4.4 virus isolates have retained only the K222Q substitution but still bind fucosylated sialosides. Altered receptor-binding specificity of virus clade 2.3.4.4 H5 proteins might have contributed to emergence and spread of H5Nx viruses. |
| Databáze: | OpenAIRE |
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