@article{SchneiderSchauliesSchnorrDunsteretal.1994,
  author    = {Schneider-Schaulies, Sibylle and Schnorr, J.-J. and Dunster, L. M. and Schneider-Schaulies, J{\"u}rgen and ter Meulen, Volker},
  title     = {The role of host factors in measles virus persistence},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-54944},
  year      = {1994},
  abstract  = {As critical steps in the life cycle oJ measles virus (Mfl), the e.fficiency of uptake into and replication in susceptible host cells are governed by cellular determinants. Measles virus infections of cells of the human CNS are characterized by particular constraints imposed on v1:ral transcription and translation attenuating viral gene Junctions and thus contributing to the pathogenesis oJ MV persistence in these cells.},
  subject      = {Immunologie},
  language  = {en}
}
@article{DunsterSchneiderSchauliesLoeffleretal.1994,
  author    = {Dunster, L.M. and Schneider-Schaulies, J{\"u}rgen and L{\"o}ffler, S. and Lankes, W. and Schwartz-Albiez, R. and Lottspeich, F. and ter Meulen, V.},
  title     = {Moesin: a cell membrane protein linked with susceptibility to measles virus infection},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-54931},
  year      = {1994},
  abstract  = {Measles virus is a highly contagious virus causing acute and persistent diseases in man, the receptor of which is still not weil characterized. We have isolated a monoclonal antibody (mAb), designated mAb 119, which specifically inhibits measles virus infection of susceptible celllines in a dosa-dependent manner. This antibody precipitates a protein with an apparent molecular mass of 75 kDa from 1251 surface-labeled cells and its epitope is present on human peripheral blood mononuclear cells, human celllines, and the African green monkey cellline Vero. Affinity chromatography of detergent-solubilized cell membrane proteins over a Sepharose column with covalently bound mAb 119 led to the partial purification of the 75-kOa protein. Preincubation of measles virus with this affinity-purified protein inhibited measles virus infection dose dependently. Aminoacid microseq,uencing of this protein revealed its identity with the human membrane-organizing extension spike protein moesin, a protein intra- and extracellularly associated with the plasma membrane of cells. Subsequently, an antibody raised against purified moesin (mAb 38/87) was also found to specifically inhibit measles virus infection of susceptible cells and confirmed our data obtained with mAb 119. Our data suggest that moesin is acting as a receptor for measles virus.},
  subject      = {Immunologie},
  language  = {en}
}