Literature DB >> 23536663

Substitutions T200A and E227A in the hemagglutinin of pandemic 2009 influenza A virus increase lethality but decrease transmission.

Carles Martínez-Romero1, Erik de Vries, Alan Belicha-Villanueva, Ignacio Mena, Donna M Tscherne, Virginia L Gillespie, Randy A Albrecht, Cornelis A M de Haan, Adolfo García-Sastre.   

Abstract

We report that swine influenza virus-like substitutions T200A and E227A in the hemagglutinin (HA) of the 2009 pandemic influenza virus alter its pathogenesis and transmission. Viral replication is increased in mammalian cells. Infected mice show increased disease as measured by weight loss and lethality. Transmission in ferrets is decreased in the presence of both substitutions, suggesting that amino acids 200T and 227E are adaptive changes in the HA of swine origin influenza viruses associated with increased transmission and decreased pathogenesis.

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Year:  2013        PMID： 23536663      PMCID： PMC3648128          DOI： 10.1128/JVI.00262-13

Source DB:  PubMed          Journal:  J Virol        ISSN： 0022-538X            Impact factor:   5.103


  10 in total

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  10 in total
  6 in total

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Authors:  Florian Krammer; Rong Hai; Mark Yondola; Gene S Tan; Victor H Leyva-Grado; Alex B Ryder; Matthew S Miller; John K Rose; Peter Palese; Adolfo García-Sastre; Randy A Albrecht
Journal:  J Virol       Date:  2014-01-08       Impact factor: 5.103

2.  Hemagglutinin Stalk Immunity Reduces Influenza Virus Replication and Transmission in Ferrets.

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3.  Evolution of the hemagglutinin protein of the new pandemic H1N1 influenza virus: maintaining optimal receptor binding by compensatory substitutions.

Authors:  Robert P de Vries; Erik de Vries; Carles Martínez-Romero; Ryan McBride; Frank J van Kuppeveld; Peter J M Rottier; Adolfo García-Sastre; James C Paulson; Cornelis A M de Haan
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5.  Characterization of swine-origin H1N1 canine influenza viruses.

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6.  Analysis of the Contrasting Pathogenicities Induced by the D222G Mutation in 1918 and 2009 Pandemic Influenza A Viruses.

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  6 in total

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