Type IV fimbrial biogenesis is required for protease secretion and natural transformation in Dichelobacter nodosus

Xiao Yan Han, Ruth May Kennan, Dane Parker, John Keith Davies, Julian Ian Rood

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Abstract

The objective of this study was to develop an understanding of the molecular mechanisms by which type IV fimbrial biogenesis, natural transformation, and protease secretion are linked in the ovine footrot pathogen Dichelobacter nodosus. We have shown that like the D. nodosus fimbrial subunit FimA, the pilin-like protein PilE and the FimN, FimO, and FimP proteins, which are homologs of PilB, PilC, and PilD from Pseudomonas aeruginosa, are essential for fimbrial biogenesis and natural transformation, indicating that transformation requires an intact type IV fimbrial apparatus. The results also showed that extracellular protease secretion in the fimN, fimO, fimP and pilE mutants was significantly reduced, which represents the first time that PilB, PilC and PilE homologs have been shown to be required for the secretion of unrelated extracellular proteins in a type IV fimbriate bacterium. Quantitative real time PCR analysis of the three extracellular proteases genes, aprV2, aprV5, and bprV, showed that the effects on protease secretion were not mediated at the transcriptional level. Bioinformatic analysis did not identify a classical type II secretion system and the putative fimbrial biogenesis gene pilQ was the only outer membrane secretin gene identified. Based on these results it is postulated that in D. nodosus protease secretion occurs by a type II secretion-related process that directly involves components of the type IV fimbrial biogenesis machinery, which represents the only type II secretion system encoded by the small genome of this highly evolved pathogen.
Original languageEnglish
Pages (from-to)5022 - 5033
Number of pages12
JournalJournal of Bacteriology
Volume189
Issue number14
Publication statusPublished - 2007

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