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Back Cover: Discovery of a Highly Selective PLD2 Inhibitor (ML395): A New Probe with Improved Physiochemical Properties and Broad‐Spectrum Antiviral Activity against Influenza Strains (ChemMedChem 12/2014)
Author(s) -
O'Reilly Matthew C.,
Oguin Thomas H.,
Scott Sarah A.,
Thomas Paul G.,
Locuson Charles W.,
Morrison Ryan D.,
Daniels J. Scott,
Brown H. Alex,
Lindsley Craig W.
Publication year - 2014
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201490047
Subject(s) - pld2 , rna interference , pathogen , nucleoprotein , interferon , biology , influenza a virus , virology , chemistry , pathogenicity , host (biology) , microbiology and biotechnology , virus , rna , biochemistry , gene , genetics , phospholipid , phosphatidic acid , membrane
The back cover picture shows a co‐localization study of A549 cells infected with influenza A virus, H1N1: influenza nucleoprotein (green), interferon‐induced protein MxA (red), phospholipase D2 (PLD2; magenta), and cell nuclei (blue). Here, we observe pathogen proteins and host PLD2 trafficking together, and these findings led to the hypothesis that PLD2 might play a role in pathogenicity. Efficient invasion is blocked by disruption of PLD activity using an inhibitor ML395 (shown) or RNA interference, suggesting that activation of host PLD2 is required for viral entry. For more details, see the Communication by Craig W. Lindsley et al. on p. 2633 ff.