Host Interactions with Influenza Factors (Homo sapiens)

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56111327-10cytosolmitochondrial inner membranemitochondrial intermembrane spacenucleoplasmGolgi lumenNS1 HomodimerSLC25A6NS1 TGFB1PB1-F2: ANT 3ComplexNS1:PAB II ComplexViral dsRNA (-)StrandedPB1-F2 NS1 HomodimerNS1 NS1 CPSF:NS1 ComplexNS1 PB1-F2SLC25A6 EIF2AK2 PABPN1CPSF4 NS1 PABPN1 EIF2AK2TGFB1(30-390)NS1:Viral dsRNAComplexNS1 Homodimer:PKRComplexCPSF4NS1 NA44


Description

Infection of a human host cell with influenza virus triggers an array of host processes that interfere with viral replication, notably the production of type I interferon. The viral NS1 protein plays a central role in these virus-host interactions. Source:Reactome.

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Bibliography

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  1. O'Neill RE, Jaskunas R, Blobel G, Palese P, Moroianu J.; ''Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import.''; PubMed Europe PMC Scholia
  2. Fortes P, Beloso A, Ortín J.; ''Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport.''; PubMed Europe PMC Scholia
  3. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
  4. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC Scholia
  5. Noah DL, Twu KY, Krug RM.; ''Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS.''; PubMed Europe PMC Scholia
  6. Li N, Ren A, Wang X, Fan X, Zhao Y, Gao GF, Cleary P, Wang B.; ''Influenza viral neuraminidase primes bacterial coinfection through TGF-β-mediated expression of host cell receptors.''; PubMed Europe PMC Scholia
  7. Son KN, Liang Z, Lipton HL.; ''Double-Stranded RNA Is Detected by Immunofluorescence Analysis in RNA and DNA Virus Infections, Including Those by Negative-Stranded RNA Viruses.''; PubMed Europe PMC Scholia
  8. Melén K, Kinnunen L, Fagerlund R, Ikonen N, Twu KY, Krug RM, Julkunen I.; ''Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.''; PubMed Europe PMC Scholia
  9. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed Europe PMC Scholia
  10. Chen Z, Li Y, Krug RM.; ''Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery.''; PubMed Europe PMC Scholia
  11. Morris SJ, Price GE, Barnett JM, Hiscox SA, Smith H, Sweet C.; ''Role of neuraminidase in influenza virus-induced apoptosis.''; PubMed Europe PMC Scholia
  12. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC Scholia
  13. Cros JF, García-Sastre A, Palese P.; ''An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein.''; PubMed Europe PMC Scholia
  14. De Marcos Lousa C, Trézéguet V, Dianoux AC, Brandolin G, Lauquin GJ.; ''The human mitochondrial ADP/ATP carriers: kinetic properties and biogenesis of wild-type and mutant proteins in the yeast S. cerevisiae.''; PubMed Europe PMC Scholia
  15. Donelan NR, Basler CF, García-Sastre A.; ''A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice.''; PubMed Europe PMC Scholia
  16. Bergmann M, Garcia-Sastre A, Carnero E, Pehamberger H, Wolff K, Palese P, Muster T.; ''Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication.''; PubMed Europe PMC Scholia
  17. Chanturiya AN, Basañez G, Schubert U, Henklein P, Yewdell JW, Zimmerberg J.; ''PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes.''; PubMed Europe PMC Scholia
  18. Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM.; ''Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs.''; PubMed Europe PMC Scholia
  19. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed Europe PMC Scholia
  20. Li Y, Chen ZY, Wang W, Baker CC, Krug RM.; ''The 3'-end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo.''; PubMed Europe PMC Scholia
  21. Shimizu K, Iguchi A, Gomyou R, Ono Y.; ''Influenza virus inhibits cleavage of the HSP70 pre-mRNAs at the polyadenylation site.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
101952view13:25, 20 November 2018EgonwRemoved an empty reference.
101205view11:10, 1 November 2018ReactomeTeamreactome version 66
100743view20:35, 31 October 2018ReactomeTeamreactome version 65
100287view19:11, 31 October 2018ReactomeTeamreactome version 64
99833view15:56, 31 October 2018ReactomeTeamreactome version 63
99390view14:33, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99087view12:39, 31 October 2018ReactomeTeamreactome version 62
93925view13:45, 16 August 2017ReactomeTeamreactome version 61
93509view11:25, 9 August 2017ReactomeTeamreactome version 61
87137view18:51, 18 July 2016MkutmonOntology Term : 'infectious disease pathway' added !
86605view09:22, 11 July 2016ReactomeTeamreactome version 56
83394view11:06, 18 November 2015ReactomeTeamVersion54
81586view13:07, 21 August 2015ReactomeTeamVersion53
77047view08:34, 17 July 2014ReactomeTeamFixed remaining interactions
76752view12:11, 16 July 2014ReactomeTeamFixed remaining interactions
76077view10:14, 11 June 2014ReactomeTeamRe-fixing comment source
75787view11:31, 10 June 2014ReactomeTeamReactome 48 Update
75137view14:08, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74784view08:52, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
CPSF4 ProteinO95639 (Uniprot-TrEMBL)
CPSF4ProteinO95639 (Uniprot-TrEMBL)
CPSF:NS1 ComplexComplexR-HSA-169074 (Reactome)
EIF2AK2 ProteinP19525 (Uniprot-TrEMBL)
EIF2AK2ProteinP19525 (Uniprot-TrEMBL)
NAProteinP03468 (Uniprot-TrEMBL)
NS1 Homodimer:PKR ComplexComplexR-HSA-169142 (Reactome)
NS1 HomodimerComplexR-FLU-169143 (Reactome)
NS1 HomodimerComplexR-FLU-169145 (Reactome)
NS1 ProteinP03496 (Uniprot-TrEMBL)
NS1:PAB II ComplexComplexR-HSA-169102 (Reactome)
NS1:Viral dsRNA ComplexComplexR-FLU-169075 (Reactome)
PABPN1 ProteinQ86U42 (Uniprot-TrEMBL)
PABPN1ProteinQ86U42 (Uniprot-TrEMBL)
PB1-F2 ProteinP0C0U1 (Uniprot-TrEMBL)
PB1-F2: ANT 3 ComplexComplexR-HSA-169235 (Reactome)
PB1-F2ProteinP0C0U1 (Uniprot-TrEMBL)
SLC25A6 ProteinP12236 (Uniprot-TrEMBL)
SLC25A6ProteinP12236 (Uniprot-TrEMBL)
TGFB1(30-390)ProteinP01137 (Uniprot-TrEMBL)
TGFB1ProteinP01137 (Uniprot-TrEMBL)
Viral dsRNA (-) StrandedR-NUL-167931 (Reactome)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
CPSF4R-HSA-168859 (Reactome)
CPSF:NS1 ComplexArrowR-HSA-168859 (Reactome)
EIF2AK2R-HSA-168896 (Reactome)
NAmim-catalysisR-HSA-168865 (Reactome)
NS1 Homodimer:PKR ComplexArrowR-HSA-168896 (Reactome)
NS1 HomodimerR-HSA-168859 (Reactome)
NS1 HomodimerR-HSA-168883 (Reactome)
NS1 HomodimerR-HSA-168891 (Reactome)
NS1 HomodimerR-HSA-168896 (Reactome)
NS1:PAB II ComplexArrowR-HSA-168883 (Reactome)
NS1:Viral dsRNA ComplexArrowR-HSA-168891 (Reactome)
PABPN1R-HSA-168883 (Reactome)
PB1-F2: ANT 3 ComplexArrowR-HSA-168878 (Reactome)
PB1-F2R-HSA-168878 (Reactome)
R-HSA-168859 (Reactome) Influenza virus's non-structural protein (NS1) binds to the host cell's cleavage and host polyadenylation specificity factor (CPSF), inhibiting the ability of CPSF to bind to pre-mRNAs and thus preventing efficient 3' end processing and export of host cell mRNAs out of the nucleus.
R-HSA-168865 (Reactome) Influenza A virus induces apoptosis in a variety of ways including by activation of host TGF-beta by viral neuraminidase (NA).
R-HSA-168878 (Reactome) Influenza A virus induces apoptosis in a variety of ways including binding of viral PB1-F2 to host mitochondrial adenine nucleotide translocator 3 (ANT3).
R-HSA-168883 (Reactome) The influenza virus non-structural protein 1 (NS1) binds to the host cell's poly(A)-binding protein II (PABII) thus preventing PABII from properly extending the poly-A tail of pre-mRNA within the host cell nucleus. These pre-mRNAs are then prevented from exiting the nucleus.
R-HSA-168891 (Reactome) The ability of viral non-structural protein 1 (NS1) to sequester dsRNA is believed to be one of the primary mechanisms by which NS1 prevents activation of downstream anti-viral signaling pathways.
R-HSA-168896 (Reactome) Influenza virus inhibits the host double-stranded-RNA-activated protein kinase (PKR) by a couple of mechanisms. One of those steps is the direct binding of PKR by the viral non-structural protein NS1.
SLC25A6R-HSA-168878 (Reactome)
TGFB1(30-390)R-HSA-168865 (Reactome)
TGFB1ArrowR-HSA-168865 (Reactome)
Viral dsRNA (-) StrandedR-HSA-168891 (Reactome)
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