The purified and recombinant Legionella pneumophila chaperonin alters mitochondrial trafficking and microfilament organization.

@article{Chong2009ThePA,
  title={The purified and recombinant Legionella pneumophila chaperonin alters mitochondrial trafficking and microfilament organization.},
  author={Audrey Chong and Celia A. Lima and D S Allan and Gheyath K. Nasrallah and Rafael A. Gardu{\~n}o},
  journal={Infection and immunity},
  year={2009},
  volume={77 11},
  pages={4724-39}
}
A portion of the total cellular pool of the Legionella pneumophila chaperonin, HtpB, is found on the bacterial cell surface, where it can mediate invasion of nonphagocytic cells. HtpB continues to be abundantly produced and released by internalized L. pneumophila and may thus have postinvasion functions. We used here two functional models (protein-coated beads and expression of recombinant proteins in CHO cells) to investigate the competence of HtpB in mimicking early intracellular trafficking… CONTINUE READING

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