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@ARTICLE{Hnel:60124,
      author       = {Hänel, K. and Willbold, D.},
      title        = {{SARS}-{C}o{V} accessory protein 7a directly interacts with
                      human {LFA}-1},
      journal      = {Biological chemistry},
      volume       = {388},
      issn         = {1431-6730},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {PreJuSER-60124},
      pages        = {1325 - 1332},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The SARS-CoV accessory protein 7a is a type I membrane
                      protein with an extracellular domain of 81 amino acid
                      residues. It is described to be expressed during infection
                      and to be a component of the virus particle surface. In this
                      study, we demonstrate that protein 7a binds directly and
                      specifically to human lymphocyte function-associated antigen
                      1 (LFA-1) on the cell surface of Jurkat cells. The binding
                      is increased upon artificial cell activation with phorbol
                      ester. These observations are confirmed by direct in vitro
                      binding of recombinant protein 7a to the wild type and
                      mutant K287C/K294C I domain showing that the I domain is the
                      7a binding site in the alpha(L) chain of LFA-1. Consequences
                      of the LFA-1 interaction with 7a are discussed. In
                      particular, our data suggest LFA-1 to be an attachment
                      factor or the receptor for SARS-CoV on human leukocytes.},
      keywords     = {Blotting, Western / Carcinogens: pharmacology / Cloning,
                      Molecular / Enzyme-Linked Immunosorbent Assay / Humans /
                      Intercellular Adhesion Molecule-1: metabolism / Jurkat Cells
                      / Lymphocyte Function-Associated Antigen-1: chemistry /
                      Mutation / Phorbol 12,13-Dibutyrate: pharmacology / Protein
                      Binding / Protein Conformation / Receptors, Cell Surface:
                      metabolism / Recombinant Proteins: chemistry / Viral Matrix
                      Proteins: chemistry / Viral Matrix Proteins: genetics /
                      Viral Proteins: chemistry / Viral Proteins: genetics /
                      Carcinogens (NLM Chemicals) / Lymphocyte Function-Associated
                      Antigen-1 (NLM Chemicals) / Receptors, Cell Surface (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) / Viral
                      Matrix Proteins (NLM Chemicals) / Viral Proteins (NLM
                      Chemicals) / sars7a protein, SARS virus (NLM Chemicals) /
                      Intercellular Adhesion Molecule-1 (NLM Chemicals) / Phorbol
                      12,13-Dibutyrate (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18020948},
      UT           = {WOS:000251393700006},
      doi          = {10.1515/BC.2007.157},
      url          = {https://juser.fz-juelich.de/record/60124},
}