Role of the Bordetella pertussis minor fimbrial subunit, FimD, in colonization of the mouse respiratory tract.
Bordetella pertussis fimbriae are composed of a major subunit, Fim2 or Fim3, and the minor subunit FimD. Using immunoelectron microscopy, we provide evidence that FimD is located at the fimbrial tip. The role of FimD in colonization of the mouse respiratory tract was studied by using two fimbrial mutants: a mutant completely devoid of fimbriae (designated FimD-) and a mutant devoid of the major fimbrial subunits but still producing the minor subunit (designated FimD+). The ability of the two fimbrial mutants to colonize the nasopharynx, trachea, and lungs was compared with those of the wild type parental strain and a filamentous hemagglutinin (FHA) mutant. Of the three mutants studied, the FimD- mutant showed the greatest defect, colonizing less well in the nasopharynx, trachea, and lungs. The most pronounced defect in colonizing ability of the three mutants was observed in the trachea. However, the colonizing defect of the FHA and FimD+ mutants in the trachea was observed only during the first 3 days of infection. After 10 days, the colonization level was nearly restored to wild-type levels. The FHA and FimD+ mutants showed a slight colonization defect in the nasopharynx but no defect in the lungs. A maltose binding protein-FimD fusion protein and a peptide derived from FimD were able to bind to heparin, a member of a class of sulfated sugars which are ubiquitous in the respiratory tract. Recently it was shown (W. L. W. Hazenbos, C. A. W. Geuijen, B. M. van den Berg, F. R. Mooi, and R. van Furth, J. Infect. Dis. 171:924-929, 1995) that FimD also binds to the integrin VLA-5, and our results suggest that the binding of B. pertussis to these two molecules plays an important role in colonization of the respiratory tract of the mouse.
Geuijen
C A
CA
Research Laboratory for Infectious Diseases, National Institute of Public Health and Environment, Bilthoven, The Netherlands.
Willems
R J
RJ
Bongaerts
M
M
Top
J
J
Gielen
H
H
Mooi
F R
FR
D018829:Adhesins, Bacterial / Q000235:genetics; D000818:Animals; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics; D001886:Bordetella pertussis / Q000472:pathogenicity* / Q000648:ultrastructure; D004195:Disease Models, Animal; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000648:ultrastructure; D006388:Hemagglutinins / Q000235:genetics; D008168:Lung / Q000382:microbiology; D051379:Mice; D008807:Mice, Inbred BALB C; D009154:Mutation; D009305:Nasopharynx / Q000382:microbiology; D011485:Protein Binding; D014132:Trachea / Q000382:microbiology; D010566:Virulence Factors, Bordetella; D014917:Whooping Cough / Q000209:etiology*
D018829:Adhesins, Bacterial; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D006388:Hemagglutinins; D010566:Virulence Factors, Bordetella; C065273:filamentous hemagglutinin adhesin, Bordetella pertussis; C101541:fim2 protein, Bordetella; C101542:fim3 protein, Bordetella; C489284:fimD protein, Bordetella; C063629:fimD protein, bacteria; D036781:Fimbriae Proteins