Abstract
Avian-origin influenza virus polymerase activity can be dramatically increased in human cells with the PB2 E627K mutation. Previously, others have proposed that this mutation increases the stability of the viral ribonucleoprotein complex (vRNP) measured by the interaction between PB2 and NP. However, we demonstrate here that a variety of PB2 adaptive mutations, including E627K, do not enhance the stability of the vRNP but rather increase the amount of replicated RNA that results in more PB2-NP coprecipitation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Birds / virology
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Cell Line
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Humans
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Influenza A virus / immunology*
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Influenza A virus / isolation & purification
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Influenza A virus / physiology*
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Influenza in Birds / virology
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Mutant Proteins / genetics
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Mutant Proteins / metabolism
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Protein Binding
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RNA-Dependent RNA Polymerase / genetics
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RNA-Dependent RNA Polymerase / metabolism*
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Ribonucleoproteins / metabolism*
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Viral Proteins / genetics
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Viral Proteins / metabolism*
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Virus Replication*
Substances
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Mutant Proteins
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PB2 protein, Influenzavirus A
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Ribonucleoproteins
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Viral Proteins
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RNA-Dependent RNA Polymerase