PandemieGrippaleV1, PascalFrancis, Curation, bibRecord, 001C12

Synergistic Adaptive Mutations in the Hemagglutinin and Polymerase Acidic Protein Lead to Increased Virulence of Pandemic 2009 H1N1 Influenza A Virus in Mice

Identifieur interne : 001C12 ( PascalFrancis/Curation ); précédent : 001C11; suivant : 001C13

Synergistic Adaptive Mutations in the Hemagglutinin and Polymerase Acidic Protein Lead to Increased Virulence of Pandemic 2009 H1N1 Influenza A Virus in Mice

Auteurs : Roman Seyer [France] ; Eike R. Hrincius [France] ; Dorothea Ritzel [Allemagne] ; Marion Abt [Allemagne] ; Alexander Mellmann [Allemagne] ; Henju Marjuki [États-Unis] ; Joachim Kühn [Allemagne] ; Thorsten Wolff [Allemagne] ; Stephan Ludwig [France] ; Christina Ehrhardt [France]

Source :

The Journal of infectious diseases [ 0022-1899 ] ; 2012.

RBID : Pascal:13-0327095

Descripteurs français

Pascal (Inist)
- Souris, Synergie, Mutation, Hémagglutinine, Protéine acide, Pathologie expérimentale, Virulence, Infection, Adaptation, Virus grippal A(H1N1).

English descriptors

KwdEn :
- Acidic protein, Adaptation, Experimental disease, Hemagglutinin, Infection, Influenzavirus A(H1N1), Mouse, Mutation, Synergism, Virulence.

Abstract

Influenza impressively reflects the paradigm of a viral disease in which continued evolution of the virus is of paramount importance for annual epidemics and occasional pandemics in humans. Because of the continuous threat of novel influenza outbreaks, it is essential to gather further knowledge about viral pathogenicity determinants. Here, we explored the adaptive potential of the influenza A virus subtype H1N1 variant isolate A/Hamburg/04/09 (HH/04) by sequential passaging in mice lungs. Three passages in mice lungs were sufficient to dramatically enhance pathogenicity of HH/04. Sequence analysis identified 4 nonsynonymous mutations in the third passage virus. Using reverse genetics, 3 synergistically acting mutations were defined as pathogenicity determinants, comprising 2 mutations in the hemagglutinin (HA[D222G] and HA[K163E]), whereby the HA(D222G) mutation was shown to determine receptor binding specificity and the polymerase acidic (PA) protein F35L mutation increasing polymerase activity. In conclusion, synergistic action of all 3 mutations results in a mice lethal pandemic H1N1 virus.

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Influenza impressively reflects the paradigm of a viral disease in which continued evolution of the virus is of paramount importance for annual epidemics and occasional pandemics in humans. Because of the continuous threat of novel influenza outbreaks, it is essential to gather further knowledge about viral pathogenicity determinants. Here, we explored the adaptive potential of the influenza A virus subtype H1N1 variant isolate A/Hamburg/04/09 (HH/04) by sequential passaging in mice lungs. Three passages in mice lungs were sufficient to dramatically enhance pathogenicity of HH/04. Sequence analysis identified 4 nonsynonymous mutations in the third passage virus. Using reverse genetics, 3 synergistically acting mutations were defined as pathogenicity determinants, comprising 2 mutations in the hemagglutinin (HA[D222G] and HA[K163E]), whereby the HA(D222G) mutation was shown to determine receptor binding specificity and the polymerase acidic (PA) protein F35L mutation increasing polymerase activity. In conclusion, synergistic action of all 3 mutations results in a mice lethal pandemic H1N1 virus.</div>
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<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Robert Koch Institute</s1>
<s2>Berlin</s2>
<s3>DEU</s3>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>8 aut.</sZ>
</fA14>
<fA14 i1="03"><s1>Institute of Hygiene</s1>
<s2>Muenster</s2>
<s3>DEU</s3>
<sZ>5 aut.</sZ>
</fA14>
<fA14 i1="04"><s1>Division of Virology, Department of Infectious Diseases, St Jude Children's Research Hospital</s1>
<s2>Memphis, Tennessee</s2>
<s3>USA</s3>
<sZ>6 aut.</sZ>
</fA14>
<fA14 i1="05"><s1>Institute of Medical Microbiology, Clinical Virology</s1>
<s2>Muenster</s2>
<s3>DEU</s3>
<sZ>7 aut.</sZ>
</fA14>
<fA20><s1>262-271</s1>
</fA20>
<fA21><s1>2012</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>2052</s2>
<s5>354000507709330150</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2013 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>45 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>13-0327095</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>The Journal of infectious diseases</s0>
</fA64>
<fA66 i1="01"><s0>GBR</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>Influenza impressively reflects the paradigm of a viral disease in which continued evolution of the virus is of paramount importance for annual epidemics and occasional pandemics in humans. Because of the continuous threat of novel influenza outbreaks, it is essential to gather further knowledge about viral pathogenicity determinants. Here, we explored the adaptive potential of the influenza A virus subtype H1N1 variant isolate A/Hamburg/04/09 (HH/04) by sequential passaging in mice lungs. Three passages in mice lungs were sufficient to dramatically enhance pathogenicity of HH/04. Sequence analysis identified 4 nonsynonymous mutations in the third passage virus. Using reverse genetics, 3 synergistically acting mutations were defined as pathogenicity determinants, comprising 2 mutations in the hemagglutinin (HA[D222G] and HA[K163E]), whereby the HA(D222G) mutation was shown to determine receptor binding specificity and the polymerase acidic (PA) protein F35L mutation increasing polymerase activity. In conclusion, synergistic action of all 3 mutations results in a mice lethal pandemic H1N1 virus.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A05C04</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Souris</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Mouse</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Ratón</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Synergie</s0>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Synergism</s0>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Sinergia</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Mutation</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Mutation</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Mutación</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Hémagglutinine</s0>
<s5>07</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Hemagglutinin</s0>
<s5>07</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Hemoaglutinina</s0>
<s5>07</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Protéine acide</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Acidic protein</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Proteína ácida</s0>
<s5>08</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Pathologie expérimentale</s0>
<s5>09</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Experimental disease</s0>
<s5>09</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Patología experimental</s0>
<s5>09</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Virulence</s0>
<s5>10</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Virulence</s0>
<s5>10</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Virulencia</s0>
<s5>10</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Infection</s0>
<s5>11</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Infection</s0>
<s5>11</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Infección</s0>
<s5>11</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Adaptation</s0>
<s5>12</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Adaptation</s0>
<s5>12</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Adaptación</s0>
<s5>12</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Virus grippal A(H1N1)</s0>
<s4>CD</s4>
<s5>97</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Influenzavirus A(H1N1)</s0>
<s4>CD</s4>
<s5>97</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fN21><s1>308</s1>
</fN21>
</pA>
</standard>
</inist>
</record>

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Synergistic Adaptive Mutations in the Hemagglutinin and Polymerase Acidic Protein Lead to Increased Virulence of Pandemic 2009 H1N1 Influenza A Virus in Mice

Synergistic Adaptive Mutations in the Hemagglutinin and Polymerase Acidic Protein Lead to Increased Virulence of Pandemic 2009 H1N1 Influenza A Virus in Mice

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