Pertussis toxin. Entry into cells and enzymatic activity.
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.
el Bayâ
A
A
Institut für Infektiologie, Universität Münster, Germany.
Linnermann
R
R
von Olleschik-Elbheim
L
L
Schmidt
M A
MA
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*
D010566:Virulence Factors, Bordetella; D000246:Adenosine Diphosphate Ribose; D037342:Pertussis Toxin; D019206:GTP-Binding Protein alpha Subunits, Gi-Go