Journal
CELL HOST & MICROBE
Volume 18, Issue 6, Pages 723-735Publisher
CELL PRESS
DOI: 10.1016/j.chom.2015.11.002
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Funding
- NIAID [U19 AI106754]
- Swiss National Science Foundation [31003A_135278]
- AXA Research Fund
- NIH [P50 GM085764]
- National Institute of Allergy and Infectious Diseases of the NIH [1R01AI091786]
- Burroughs Wellcome Fund
- Bill and Melinda Gates Foundation
- Swiss National Science Foundation (SNF) [31003A_135278] Funding Source: Swiss National Science Foundation (SNF)
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Several systems-level datasets designed to dissect host-pathogen interactions during influenza A infection have been reported. However, apparent discordance among these data has hampered their full utility toward advancing mechanistic and therapeutic knowledge. To collectively reconcile these datasets, we performed a meta-analysis of data from eight published RNAi screens and integrated these data with three protein interaction datasets, including one generated within the context of this study. Further integration of these data with global virus-host interaction analyses revealed a functionally validated biochemical landscape of the influenza-host interface, which can be queried through a simplified and customizable web portal (http://www.metascape.org/IAV). Follow-up studies revealed that the putative ubiquitin ligase UBR4 associates with the viral M2 protein and promotes apical transport of viral proteins. Taken together, the integrative analysis of influenza OMICs datasets illuminates a viral-host network of high-confidence human proteins that are essential for influenza A virus replication.
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