Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin.

@article{McClain2003EssentialRO,
  title={Essential role of a GXXXG motif for membrane channel formation by Helicobacter pylori vacuolating toxin.},
  author={Mark S McClain and Hideki Iwamoto and Ping Cao and Arlene D Vinion-Dubiel and Yi Li and G{\'a}bor Szab{\'o} and Zhifeng Shao and Timothy L Cover},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 14},
  pages={12101-8}
}
Helicobacter pylori secretes a toxin, VacA, that can form anion-selective membrane channels. Within a unique amino-terminal hydrophobic region of VacA, there are three tandem GXXXG motifs (defined by glycines at positions 14, 18, 22, and 26), which are characteristic of transmembrane dimerization sequences. The goals of the current study were to investigate whether these GXXXG motifs are required for membrane channel formation and cytotoxicity and to clarify the role of membrane channel… CONTINUE READING