Structure Basis for a Subunit Interaction of Influenza Virus RNA Polymerase for Drug Design

DOI:10.15011//jasma.34.340107
Int. J. Microgravity Sci. Appl. 2017p340107
Author
Hisashi YOSHIDA and Sam-Yong PARK
Organization
Kanagawa Academy of Science and Technology,
Abstract
Influenza A virus is a major human and animal pathogen with the potential to cause catastrophic loss of life. Influenza virus reproduces rapidly, mutates frequently, and occasionally crosses species barriers. The recent emergence of swine-origin influenza H1N1 and avian influenza related to highly pathogenic forms of the human virus has highlighted the urgent need for new effective treatments. Here, we describe two crystal structures of complexes made by fragments of PA and PB1, and PB1 and PB2. These novel interfaces are surprisingly small, yet they play a crucial role in regulating the 250 kDa. polymerase complex, and are completely conserved among swine, avian and human influenza viruses. Given their importance to viral replication and strict conservation, the PA/PB1 and PB1/PB2 interfaces appear to be promising targets for novel anti-influenza drugs of use against all strains of influenza A virus. It is hoped that the structures presented here will assist the search for such compounds.
Keyword(s)
Influenza virus, RNA polymerase, X-ray crystallographic
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Received 1 August 2016, Accepted 11 January 2017, Published 31 January 2017

© The Japan Society of Microgravity Applicaiton

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