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@ARTICLE{Dupr:634624,
      author       = {Dupré, Juliette and Dolata, Katarzyna Magdalena and Pei,
                      Gang and Molouki, Aidin and Goatley, Lynnette C. and
                      Küchler, Richard and Soh, Timothy K. and Bosse, Jens
                      Bernhard and Fablet, Aurore and Le Dimna, Mireille and
                      Karadjian, Grégory and Hirchaud, Edouard and Netherton,
                      Christopher L. and Dixon, Linda K. and Reis, Ana Luisa and
                      Vitour, Damien and Le Potier, Marie-Frédérique and Karger,
                      Axel and Caignard, Grégory},
      title        = {{E}xploring virus-host interactions through combined
                      proteomic approaches identifies {BANF}1 as a new essential
                      factor for {A}frican {S}wine {F}ever {V}irus},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {24},
      number       = {9},
      issn         = {1535-9476},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {PUBDB-2025-02538},
      pages        = {101038},
      year         = {2025},
      abstract     = {African swine fever virus (ASFV) causes a lethal disease in
                      pigs and represents a significant threat to the global pork
                      industry due to the lack of effective vaccines or
                      treatments. Despite intensive research, many ASFV proteins
                      remain uncharacterized. This study aimed to elucidate the
                      functions of two ASFV proteins, pMGF360-21R and pA151R,
                      through comprehensive analysis of their interactions with
                      host proteins. Using affinity purification-mass spectrometry
                      and yeast two-hybrid screening approaches, we identified the
                      host protein barrier-to-autointegration factor 1 (BANF1) as
                      a key interactor of both viral proteins. Biochemical and
                      colocalization assays confirmed these interactions and
                      demonstrated that MGF360-21R and A151R expression leads to
                      cytoplasmic relocation of BANF1. Functionally, BANF1
                      silencing significantly reduced ASFV replication, indicating
                      its proviral role. Given BANF1's established function in
                      regulating the cGAS/STING-dependent type I interferon
                      (IFN-I) response, we postulated that A151R and MGF360-21R
                      could inhibit this pathway. Using different strategies, we
                      showed that both A151R and MGF360-21R did indeed inhibit
                      IFN-I induction. Generation of ASFV deficient of A151R or
                      MGF360-21R showed that both mutant viruses enhanced the host
                      IFN response in primary porcine macrophages compared to
                      wild-type virus. However, their capacity to inhibit this
                      pathway could occur through mechanisms independent of BANF1.
                      Proteomic analysis of BANF1 interactors during ASFV
                      infection highlighted potentially roles in chromatin
                      remodeling, nuclear transport, and innate immune response
                      pathways. Altogether, our data provide new insights into
                      ASFV-host interactions, identifying BANF1 as an important
                      new host factor required for replication and uncovering
                      novel functions for A151R and MGF360-21R.},
      cin          = {CSSB-MHH-JB},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-MHH-JB-20210520},
      pnm          = {899 - ohne Topic (POF4-899) / DFG project
                      G:(GEPRIS)390874280 - EXC 2155: RESIST - Resolving Infection
                      Susceptibility (390874280) / GRK 2771 - GRK 2771: Mensch und
                      Mikrobe: Reorganisation von Zellkompartimenten und
                      Molekülkomplexen während der Infektion (453548970) / ICRAD
                      - INTERNATIONAL COORDINATION OF RESEARCH ON INFECTIOUS
                      ANIMAL DISEASES (862605)},
      pid          = {G:(DE-HGF)POF4-899 / G:(GEPRIS)390874280 /
                      G:(GEPRIS)453548970 / G:(EU-Grant)862605},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1016/j.mcpro.2025.101038},
      url          = {https://bib-pubdb1.desy.de/record/634624},
}