2009
DOI: 10.1016/j.cell.2009.12.018
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A Physical and Regulatory Map of Host-Influenza Interactions Reveals Pathways in H1N1 Infection

Abstract: Summary During the course of a viral infection, viral proteins interact with an array of host proteins and pathways. Here we present a systematic strategy to elucidate the dynamic interactions between H1N1 influenza and its human host. A combination of yeast two hybrid analysis and genome-wide expression profiling implicated hundreds of human factors in mediating viral-host interactions. These factors were then examined functionally through depletion analyses in primary lung cells. The resulting data point to … Show more

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Cited by 596 publications
(705 citation statements)
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“…As NEP has been suggested to interact with the viral polymerase proteins in a yeast two-hybrid-screening 21, and our results suggest that it might compensate for a defect in the viral Relative activity (%) -P B 2 A v i a n P r K A N -1 V n -1 2 0 3…”
Section: Pb2-e627k Compensates For a Defect In Viral Rna Replicationmentioning
confidence: 51%
“…As NEP has been suggested to interact with the viral polymerase proteins in a yeast two-hybrid-screening 21, and our results suggest that it might compensate for a defect in the viral Relative activity (%) -P B 2 A v i a n P r K A N -1 V n -1 2 0 3…”
Section: Pb2-e627k Compensates For a Defect In Viral Rna Replicationmentioning
confidence: 51%
“…For pulse-chase analyses, HEK293FT cells were plated and transfected in 6-well plates. At 47 h posttransfection, the cells were starved in methionine-and cysteinedeficient medium for 1 h and pulsed for 1 h with medium containing 35 The resulting extract was passed through a 29½-gauge needle several times, spun down at 15,000 ϫ g for 10 min at 4°C, and immunoprecipitated by incubation overnight at 4°C with 2 g of anti-T7 MAb (Novagen), 2 g of anti-GFP MAb (Santa Cruz Biotechnology Inc.), and 20 l of a 50% bead slurry of protein A/G Plus-agarose (Santa Cruz Biotechnology Inc.). The beads were washed 4 times with 1ϫ PBS-T and resuspended in 25 l of 2ϫ sample buffer.…”
Section: Methodsmentioning
confidence: 99%
“…First, we demonstrated that besides NS1, 4 additional viral proteins are SUMOylated in vivo, including M1, PB1, NP, and NEP (NS2), and many of the predicted SUMOylation sites in these proteins appear to be fairly well conserved (32). Second, large screenings looking for host proteins that are either required for viral multiplication or capable of interacting with specific viral proteins and required for optimal virus growth identified various members of the cellular SUMOylation system (34,35). Finally, the last level of supporting information was obtained by other groups while studying the SUMOylation of specific influenza virus proteins: Xu et al confirmed our initial identification of NS1 as a SUMOylation target, mapped one SUMOylation site in NS1, and assigned a potential role for NS1 SUMOylation, namely, extending NS1's half-life (36).…”
mentioning
confidence: 99%
“…The elucidation of how influenza viruses interact with the host cell machinery and hijack cellular pathways has become an active field of research and could pave the way to new antiviral approaches targeting virus-host interactions (1,2). Several RNAi-based genome-wide screens have been performed for the identification of host factors involved in influenza virus replication (3)(4)(5)(6)(7)(8)(9). Because influenza virus polymerase is a key component in the viral life cycle and is a strong determinant of virulence and host range (10,11), other studies have used yeast two-hybrid (9,12) or proteomics approaches (13)(14)(15) to attempt to identify cellular proteins that interact with the viral polymerase.…”
mentioning
confidence: 99%