The Moraxella catarrhalis autotransporter McaP is a conserved surface protein that mediates adherence to human epithelial cells through its N-terminal passenger domain.

@article{Lipski2007TheMC,
  title={The Moraxella catarrhalis autotransporter McaP is a conserved surface protein that mediates adherence to human epithelial cells through its N-terminal passenger domain.},
  author={Serena L Lipski and Christine Akimana and Jennifer M Timpe and Ronald Mark Wooten and Eric R. Lafontaine},
  journal={Infection and immunity},
  year={2007},
  volume={75 1},
  pages={314-24}
}
The protein McaP was previously shown to be an adhesin expressed by the Moraxella catarrhalis strain O35E, which also displays esterase and phospholipase B activities (J. M. Timpe et al., Infect. Immun. 71:4341-4350, 2003). In the present study, sequence analysis suggests that McaP is a conventional autotransporter protein that contains a 12-stranded beta-barrel transporter module (amino acids [aa] 383 to 650) linked to a surface-exposed passenger domain exhibiting lipolytic activity (aa 62 to… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 30 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 67 references

Structure of the translocator domain of a bacterial autotransporter

  • C. J. Oomen, P. Van Ulsen, P. Van Gelder, M. Feijen, J. Tommassen, P. Gros
  • EMBO J. 23:1257–1266
  • 2004
Highly Influential
5 Excerpts

Similar Papers

Loading similar papers…