Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9121293 | FEMS Microbiology Letters | 2005 | 7 Pages |
Abstract
Pseudomonas aeruginosa, a Gram-negative opportunistic pathogen, translocates exoenzymes (Exo) directly into the eukaryotic cell cytoplasm. This is accomplished by a type III secretion/translocation machinery. Here, we show that the P. aeruginosa type III secretory needle structure is composed essentially of PscF, a protein required for secretion and P. aeruginosa cytotoxicity. Partially purified needles, detached from the bacterial surface, are 60-80Â nm in length and 7Â nm in width, resembling needles from Yersinia spp.. YscF of Yersinia enterocolitica was able to functionally complement the pscF deletion, but required 11 P. aeruginosa-specific amino acids at the N-terminus for its function.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Genetics
Authors
Alexandrine Pastor, Jacqueline Chabert, Mathilde Louwagie, Jerôme Garin, Ina Attree,