title: Pertussis toxin. Entry into cells and enzymatic activity.
abstract: In this study we present data supporting the concept of a retrograde transport mechanism for pertussis toxin to the Golgi complex. We also describe a novel GTP-binding 32 kDa cellular target protein, which is ADP-ribosylated upon exposure to PT and different from the classical PT substrate, the alpha-subunit of Gi proteins.
authors.affiliation: Institut für Infektiologie, Universität Münster, Germany.
authors.forename: A
authors.initials: A
authors.lastname: el Bayâ
authors.forename: R
authors.initials: R
authors.lastname: Linnermann
authors.forename: L
authors.initials: L
authors.lastname: von Olleschik-Elbheim
authors.forename: M A
authors.initials: MA
authors.lastname: Schmidt
mesh_terms: D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D016466:CHO Cells; D002460:Cell Line; D006224:Cricetinae; D004285:Dogs; D019206:GTP-Binding Protein alpha Subunits, Gi-Go / Q000378:metabolism; D037342:Pertussis Toxin; D010566:Virulence Factors, Bordetella / Q000378:metabolism*
chemical_list: D010566:Virulence Factors, Bordetella; D000246:Adenosine Diphosphate Ribose; D037342:Pertussis Toxin; D019206:GTP-Binding Protein alpha Subunits, Gi-Go