Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation.

@article{Jursch1994HistidineRN,
  title={Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation.},
  author={R Jursch and Alan Hildebrand and Gerd Hobom and J{\"O}RGEN TRANUM-JENSEN and Robert D. Ward and Michael Kehoe and Sucharit Bhakdi},
  journal={Infection and immunity},
  year={1994},
  volume={62 6},
  pages={2249-56}
}
Chemical modification of histidine residues in staphylococcal alpha-toxin leads to loss of functional activity. Site-directed mutants of the toxin in which each of the four histidine residues was replaced by several amino acids were therefore produced. The mutant proteins were purified and characterized. Exchange of H-259 or H-144 was sometimes tolerated without reduction in hemolytic activity. These histidine residues are thus not essential for toxin function. Exchange of H-35 and H-48… CONTINUE READING