Identification of fimbrial assembly genes from Dichelobacter nodosus: evidence that fimP encodes the type-IV prepilin peptidase.
Dichelobacter nodosus (Dn) is the causative agent of footrot, an economically significant disease of sheep. One of the factors believed to be involved in the virulence of this organism is its ability to produce type-IV fimbriae, which are the major protective antigens. To investigate the process of fimbrial biogenesis in Dn, gene probes were constructed from pilus biogenesis genes of Pseudomonas aeruginosa (Pa) and used to isolate homologues from Dn. A homologue, designated fimP, of the Pa prepilin peptidase-encoding gene, pilD, was cloned using this approach. The fimP gene product was shown to possess endopeptidase activity when produced in Escherichia coli. Two other fimbrial biogenesis genes fimN and fimO, whose products show similarity to the Pa PilB and PilC proteins, respectively, were identified because of their linkage to fimP. The arrangement of fimN, fimO and fimP in Dn closely resembles the arrangement of pilB, pilC and pilD in Pa.
Johnston
J L
JL
Department of Microbiology, Monash University, Clayton, Australia.
Billington
S J
SJ
Haring
V
V
Rood
J I
JI
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D010450:Endopeptidases; D004926:Escherichia coli / Q000235:genetics; D010861:Fimbriae, Bacterial / Q000235:genetics*; D005798:Genes, Bacterial; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010450:Endopeptidases; C067127:prepilin peptidase protein, Bacteria