Molecular characterization of Bordetella bronchiseptica filamentous haemagglutinin and its secretion machinery.
Two closely related pathogens, Bordetella pertussis and Bordetella bronchiseptica, share a number of virulence factors. Filamentous haemagglutinin (FHA) is widely regarded as the dominant adhesin of B. pertussis, and its multiple binding activities have been well characterized. This large protein is produced and secreted at high levels by B. pertussis and significantly lower levels by B. bronchiseptica strains. FHA secretion is mediated by a single outer-membrane accessory protein, FhaC. The genes encoding FHA and FhaC in B. bronchiseptica were characterized by sequencing and functional analyses and are highly similar to those of B. pertussis. The most distinctive feature of B. bronchiseptica FHA is additional repeats in the N-terminal portion of the predicted protein. Interestingly, a point mutation in the fhaB promoter region of the B. bronchiseptica GP1 isolate, relative to other isolates, was found to be detrimental to promoter activity and to FHA production. FhaC and the N-terminal secretion domain of FHA of B. bronchiseptica were fully functional for secretion in B. pertussis. Thus, the different levels of FHA secretion by these Bordetella species might reflect differences in physiology, composition and structure of cell envelope, or differential protein degradation. Characterization of FHA expression and function may provide clues as to the basis of host species tropism, tissue localization and receptor recognition.
Jacob-Dubuisson
Françoise
F
INSERM U447, Institut de Biologie de Lille1 and Département de Microbiologie des Ecosystèmes, Institut Pasteur de Lille2, 1 rue Calmette, F-59019 Lille Cedex, France.
Kehoe
Bettina
B
VA Palo Alto Health Care System 154T, 3801 Miranda Avenue, Palo Alto, CA 94304, USA4.|Departments of Medicine and Microbiology & Immunology, Stanford University, Stanford, CA 94305, USA3.
Willery
Eve
E
INSERM U447, Institut de Biologie de Lille1 and Département de Microbiologie des Ecosystèmes, Institut Pasteur de Lille2, 1 rue Calmette, F-59019 Lille Cedex, France.
Reveneau
Nathalie
N
INSERM U447, Institut de Biologie de Lille1 and Département de Microbiologie des Ecosystèmes, Institut Pasteur de Lille2, 1 rue Calmette, F-59019 Lille Cedex, France.
Locht
Camille
C
INSERM U447, Institut de Biologie de Lille1 and Département de Microbiologie des Ecosystèmes, Institut Pasteur de Lille2, 1 rue Calmette, F-59019 Lille Cedex, France.
Relman
David A
DA
VA Palo Alto Health Care System 154T, 3801 Miranda Avenue, Palo Alto, CA 94304, USA4.|Departments of Medicine and Microbiology & Immunology, Stanford University, Stanford, CA 94305, USA3.
D018829:Adhesins, Bacterial / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D001884:Bordetella / Q000737:chemistry / Q000235:genetics; D016950:Bordetella bronchiseptica / Q000737:chemistry / Q000235:genetics*; D001886:Bordetella pertussis / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005798:Genes, Bacterial; D049452:Green Fluorescent Proteins; D006168:Guinea Pigs; D006388:Hemagglutinins / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D015151:Immunoblotting; D008164:Luminescent Proteins / Q000032:analysis / Q000235:genetics; D008969:Molecular Sequence Data; D017354:Point Mutation; D011401:Promoter Regions, Genetic; D010566:Virulence Factors, Bordetella
D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D006388:Hemagglutinins; D008164:Luminescent Proteins; D010566:Virulence Factors, Bordetella; C098052:fhaC protein, Bordetella pertussis; C065273:filamentous hemagglutinin adhesin, Bordetella pertussis; D049452:Green Fluorescent Proteins