Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin
Carlos Espinosa-Viñals, Jiří Mašín, Jana Holubová, Ondřej Staněk, David Jurnečka, Radim Osička, Peter Šebo, Ladislav Bumba
Abstract
toxin bound and penetrated erythrocytes and CR3-expressing cells, showing that the deleted portions of RTX blocks III, IV, and V (residues 1295-1561) were dispensable for CR3 binding and for toxin translocation across the target cell membrane. This suggests that almost a half of the RTX domain of CyaA is not involved in target cell interaction and rather serves the purpose of toxin secretion.
Topics & Concepts
ChemistryBordetella pertussisToxinAdenylate Cyclase ToxinReceptorCyclaseLinkerBiophysicsAdenylate kinaseBiochemistryPertussis toxinBiologyG proteinBacteriaGeneticsOperating systemComputer scienceBacterial Infections and VaccinesLipid Membrane Structure and BehaviorBiochemical and Structural Characterization