Neuraminidase-mediated haemagglutination of recent human influenza A(H3N2) viruses is determined by arginine 150 flanking the neuraminidase catalytic site.

Mögling, Ramona; Richard, Mathilde J; Vliet, Stefan van der; Beek, Ruud van; Schrauwen, Eefje J A; Spronken, Monique I; Rimmelzwaan, Guus F; Fouchier, Ron A M

Mögling, Ramona; Richard, Mathilde J; Vliet, Stefan van der; Beek, Ruud van; Schrauwen, Eefje J A; Spronken, Monique I; Rimmelzwaan, Guus F; Fouchier, Ron A M.

Afiliación

Mögling R; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.
Richard MJ; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.
Vliet SV; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.
Beek RV; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.
Schrauwen EJA; Laboratory for Microbiology and Infection Control, Amphia Hospital, Breda, The Netherlands.
Spronken MI; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.
Rimmelzwaan GF; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.
Fouchier RAM; Department of Viroscience, Erasmus MC, Rotterdam, The Netherlands.

J Gen Virol ; 98(6): 1274-1281, 2017 Jun.

Article en En | MEDLINE | ID: mdl-28612701

RESUMEN

Over the last decade, an increasing proportion of circulating human influenza A(H3N2) viruses exhibited haemagglutination activity that was sensitive to neuraminidase inhibitors. This change in haemagglutination as compared to older circulating A(H3N2) viruses prompted an investigation of the underlying molecular basis. Recent human influenza A(H3N2) viruses were found to agglutinate turkey erythrocytes in a manner that could be blocked with either oseltamivir or neuraminidase-specific antisera, indicating that agglutination was driven by neuraminidase, with a low or negligible contribution of haemagglutinin. Using representative virus recombinants it was shown that the haemagglutinin of a recent A(H3N2) virus indeed had decreased activity to agglutinate turkey erythrocytes, while its neuraminidase displayed increased haemagglutinating activity. Viruses with chimeric and mutant neuraminidases were used to identify the amino acid substitution histidine to arginine at position 150 flanking the neuraminidase catalytic site as the determinant of this neuraminidase-mediated haemagglutination. An analysis of publicly available neuraminidase gene sequences showed that viruses with histidine at position 150 were rapidly replaced by viruses with arginine at this position between 2005 and 2008, in agreement with the phenotypic data. As a consequence of neuraminidase-mediated haemagglutination of recent A(H3N2) viruses and poor haemagglutination via haemagglutinin, haemagglutination inhibition assays with A(H3N2) antisera are no longer useful to characterize the antigenic properties of the haemagglutinin of these viruses for vaccine strain selection purposes. Continuous monitoring of the evolution of these viruses and potential consequences for vaccine strain selection remains important.

Asunto(s)

Arginina/metabolismo; Hemaglutinación; Subtipo H3N2 del Virus de la Influenza A/enzimología; Neuraminidasa/metabolismo; Animales; Arginina/genética; Dominio Catalítico; Análisis Mutacional de ADN; Eritrocitos; Evolución Molecular; Pruebas de Inhibición de Hemaglutinación; Humanos; Subtipo H3N2 del Virus de la Influenza A/genética; Gripe Humana/virología; Neuraminidasa/genética; Recombinación Genética; Genética Inversa; Pavos

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginina / Subtipo H3N2 del Virus de la Influenza A / Hemaglutinación / Neuraminidasa Límite: Animals / Humans Idioma: En Revista: J Gen Virol Año: 2017 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Reino Unido

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