% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Jarahian:170400,
      author       = {M. Jarahian and K. Marstaller$^*$ and N. Banna$^*$ and R.
                      Ahani and M. H. Etemadzadeh and L. K. Boller and K.
                      Azadmanesh and A. Cid-Arregui$^*$ and A. Khezri and M. R.
                      Berger$^*$ and F. Momburg$^*$ and C. Watzl},
      title        = {{A}ctivating {N}atural {K}iller {C}ell {R}eceptors,
                      {S}electins, and {I}nhibitory {S}iglecs {R}ecognize
                      {E}bolavirus {G}lycoprotein.},
      journal      = {Journal of innate immunity},
      volume       = {14},
      number       = {2},
      issn         = {1662-8128},
      address      = {Sydney},
      publisher    = {Karger},
      reportid     = {DKFZ-2021-01907},
      pages        = {135-147},
      year         = {2022},
      note         = {#EA:G401# / 2022;14(2):135-147},
      abstract     = {Expression of the extensively glycosylated Ebolavirus
                      glycoprotein (EBOV-GP) induces physical alterations of
                      surface molecules and plays a crucial role in viral
                      pathogenicity. Here we investigate the interactions of
                      EBOV-GP with host surface molecules using purified EBOV-GP,
                      EBOV-GP-transfected cell lines, and EBOV-GP-pseudotyped
                      lentiviral particles. Subsequently, we wanted to examine
                      which receptors are involved in this recognition by binding
                      studies to cells transfected with the EBOV-GP as well as to
                      recombinant soluble EBOV-GP. As the viral components can
                      also bind to inhibitory receptors of immune cells (e.g.,
                      Siglecs, TIM-1), they can even suppress the activity of
                      immune effector cells. Our data show that natural killer
                      (NK) cell receptors NKp44 and NKp46, selectins (CD62E/P/L),
                      the host factors DC-SIGNR/DC-SIGN, and inhibitory Siglecs
                      function as receptors for EBOV-GP. Our results show also
                      moderate to strong avidity of homing receptors (P-, L-, and
                      E-selectin) and DC-SIGNR/DC-SIGN to purified EBOV-GP, to
                      cells transfected with EBOV-GP, as well as to the envelope
                      of a pseudotyped lentiviral vector carrying the EBOV-GP. The
                      concomitant activation and inhibition of the immune system
                      exemplifies the evolutionary antagonism between the immune
                      system and pathogens. Altogether these interactions with
                      activating and inhibitory receptors result in a reduced NK
                      cell-mediated lysis of EBOV-GP-expressing cells. Modulation
                      of these interactions may provide new strategies for
                      treating infections caused by this virus.},
      keywords     = {Ebolavirus glycoprotein (Other) / HPV (Other) / Natural
                      cytotoxicity receptors (Other) / Selectins (Other) / Siglecs
                      (Other)},
      cin          = {G401 / D122 / D121},
      ddc          = {610},
      cid          = {I:(DE-He78)G401-20160331 / I:(DE-He78)D122-20160331 /
                      I:(DE-He78)D121-20160331},
      pnm          = {314 - Immunologie und Krebs (POF4-314)},
      pid          = {G:(DE-HGF)POF4-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34425576},
      doi          = {10.1159/000517628},
      url          = {https://inrepo02.dkfz.de/record/170400},
}