Infect Immun, March 1998, p. 1000-1007, Vol. 66, No. 3
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Department of Medicine/Infectious Diseases1 and Interdisciplinary Center for Biotechnology Research,2 University of Florida, Gainesville, Florida 32610, and Department of Microbiology, University of Washington, Seattle, Washington 981953
Received 9 October 1997/Returned for modification 24 November 1997/Accepted 19 December 1997
Mucin-specific adhesion of Pseudomonas aeruginosa plays
an important role in the initial colonization of this organism in the
airways of cystic fibrosis patients. We report here that the flagellar
cap protein, FliD, participates in this adhesion process. A polar chromosomal insertional mutation in the P. aeruginosa fliD gene made this organism nonadhesive to mucin in an in vitro mucin adhesion assay. The adhesive phenotype was restored by providing the fliD gene alone on a multicopy plasmid, suggesting
involvement of this gene in mucin adhesion of P. aeruginosa. Further supporting this observation, the in vitro
competition experiments demonstrated that purified FliD protein
inhibited the mucin adhesion of nonpiliated P. aeruginosa
PAK-NP, while the same concentrations of PilA and FlaG
proteins of P. aeruginosa were ineffective in this
function. The regulation of the fliD gene was studied and
was found to be unique in that the transcription of the
fliD gene was independent of the flagellar sigma factor
28. Consistent with this finding, no
28
binding sequence could be identified in the fliD promoter
region. The results of the
-galactosidase assays suggest that the
fliD gene in P. aeruginosa is regulated by the
newly described transcriptional regulator FleQ and the alternate sigma
factor
54 (RpoN).
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