Y155H amino acid substitution in influenza A(H1N1)pdm09 viruses does not confer a phenotype of reduced susceptibility to neuraminidase inhibitors

The Y155H amino acid substitution in the neuraminidase gene (NA) has previously been associated with highly reduced inhibition by neuraminidase inhibitors in the seasonal H1N1 influenza A virus which circulated in humans before the 2009 pandemic. During the 2012/13 epidemic season in Spain, two A(H1...

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Detalles Bibliográficos
Autores: Perez-Sautu, Unai, Pozo Sanchez, Francisco, Cuesta de la Plaza, Isabel, Monzon-Fernandez, Sara, Calderon-Reñon, Ana Maria, Gonzalez, M, Molinero, Mar, López-Miragaya, Isabel, Rey, Sonia, Cañizares, A, Rodriguez, G, Gonzalez-Velasco, C, Lackenby, A, Casas Flecha, Inmaculada
Tipo de recurso: artículo
Fecha de publicación:2014
País:España
Institución:Instituto de Salud Carlos III (ISCIII)
Repositorio:Repisalud
Idioma:inglés
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/9001
Acceso en línea:http://hdl.handle.net/20.500.12105/9001
Access Level:acceso abierto
Palabra clave:Amino Acid Substitution
Antiviral Agents
Drug Resistance, Viral
Enzyme Inhibitors
Female
Humans
Immunoenzyme Techniques
Influenza A Virus, H1N1 Subtype
Influenza, Human
Male
Microbial Sensitivity Tests
Neuraminidase
Oseltamivir
Pandemics
Phenotype
RNA, Viral
Seasons
Sequence Analysis, DNA
Spain
Viral Proteins
Zanamivir
Descripción
Sumario:The Y155H amino acid substitution in the neuraminidase gene (NA) has previously been associated with highly reduced inhibition by neuraminidase inhibitors in the seasonal H1N1 influenza A virus which circulated in humans before the 2009 pandemic. During the 2012/13 epidemic season in Spain, two A(H1N1) pdm09 viruses bearing the specific Y155H substitution in the NA were detected and isolated from two patients diagnosed with severe respiratory syndrome and pneumonia requiring admission to the intensive care unit. Contrary to what was observed in the seasonal A(H1N1) viruses, neither of the Y155H A(H1N1) pdm09 viruses described here showed a phenotype of reduced inhibition by NAIs as determined by the neuraminidase enzyme inhibition assay (MUNANA). High-throughput sequencing of the NA of both Y155H viruses showed that they were composed to >99% of H155 variants. We believe that this report can contribute to a better understanding of the biological significance of amino acid substitutions in the neuraminidase protein with regard to susceptibility of influenza viruses to neuraminidase inhibitors. This is of critical importance for optimal management of influenza disease patients.

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