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). Issue 12 (December 2014)

• Record Type: Journal Article
• Authors: 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.
• Is Part Of: ChemMedChem. Volume 9:Issue 12(2014:Dec.)
• Page Start: 2820
• Page End: 2820
• Publication Date: 2014-12
• Subjects: Pharmaceutical chemistry -- Periodicals; 615.19005
• DOI: 10.1002/cmdc.201490047
• Languages: English
• ISSNs: 1860-7179

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The back cover picture shows</bold> 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 <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 2633 ff.</ext-link><boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgh2cnf9m4q" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>