NDLI: Structural analysis of H1N1 and H7N9 influenza A virus PA in the absence of PB1

Content Provider	PubMed Central
Author	Moen, Spencer O. Abendroth, Jan Fairman, James W. Baydo, Ruth O. Bullen, Jameson Kirkwood, Jennifer L. Barnes, Steve R. Raymond, Amy C. Begley, Darren W. Henkel, Greg Mccormack, Ken Tam, Vincent C. Phan, Isabelle Staker, Bart L. Stacy, Robin Myler, Peter J. Lorimer, Don Edwards, Thomas E.
Copyright Year	2014
Abstract	Influenza A viruses cause the respiratory illness influenza, which can be mild to fatal depending on the strain and host immune response. The flu polymerase acidic (PA), polymerase basic 1 (PB1), and polymerase basic 2 (PB2) proteins comprise the RNA-dependent RNA polymerase complex responsible for viral genome replication. The first crystal structures of the C-terminal domain of PA (PA-CTD) in the absence of PB1-derived peptides show a number of structural changes relative to the previously reported PB1-peptide bound structures. The human A/WSN/1933 (H1N1) and avian A/Anhui1/2013 (H7N9) strain PA-CTD proteins exhibit the same global topology as other strains in the absence of PB1, but differ extensively in the PB1 binding pocket including a widening of the binding groove and the unfolding of a β-turn. Both PA-CTD proteins exhibited a significant increase in thermal stability in the presence of either a PB1-derived peptide or a previously reported inhibitor in differential scanning fluorimetry assays. These structural changes demonstrate plasticity in the PA-PB1 binding interface which may be exploited in the development of novel therapeutics.
Related Links	http://dx.doi.org/10.1038/srep05944
Starting Page	5944
File Format	PDF
ISSN	20452322
e-ISSN	20452322
Journal	Scientific Reports
Volume Number	4
Language	English
Publisher	Nature Publishing Group
Publisher Date	2014-08-01
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Science and technology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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