Bordetella pertussis Serotypes in the United States

Eldering, Grace; Holwerda, Jack; Davis, Ausma; Baker, Julia M

doi:10.1128/aem.18.4.618-621.1969

Cited by 18 publications

(8 citation statements)

References 6 publications

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“…Control mouse serum had agglutination titers of <20 with all of the given strains of B. pertussis. b Each strain of B. pertussis was typed by the agglutination assay described in the text, with typing sera prepared by G. Eldering (8,9). c Each serum was a pool from 10 mice and was mixed for 1 min at 23°C with an equal volume of 25% kaolin (0.1 to 4 ,um; Sigma Chemical Co., St. Louis, Mo.)…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae

Cowell¹,

Zhang²,

Urisu³

et al. 1987

Infect Immun

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Fimbriae were removed from Bordetella pertussis (serotype 1.3.6) by mechanical shearing and purified by precipitation with ammonium sulfate, pH-dependent precipitation at pH 7.4, followed by two successive extractions of the precipitated fimbriae with 4 M urea. By electron microscopy, the precipitated fimbriae appeared as aggregated bundles of long, relatively straight filaments which were disaggregated to individual flexuous filaments at pH 10.5. These purified fimbriae were identified as serotype 6 agglutinogens, since antibody to the purified fimbriae agglutinated B. pertussis strains serotyped as 1.3.6, 1.2.3.6, or 1.2.3.4.6 but did not agglutinate strains of serotype 1.2.3.4, 1.2.3, or 1.3. In contrast, antibody to serotype 2 fimbriae only agglutinated B. pertussis strains containing serotype 2 agglutinogen. Purified type 6 and 2 fimbriae were found to be weakly cross-reactive by enzyme-linked immunosorbent assay, using polyclonal antibody to each type of fimbria. In an immunoblot assay, polyclonal antibodies to a 22,000-dalton subunit of fimbriae from B. bronchiseptica reacted strongly with the type 2 fimbrial subunit of B. pertussis, but only weakly with the type 6 subunit. When subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the protein subunit of the type 6 fimbriae migrated with a molecular weight of 21,500, whereas the type 2 fimbrial subunit had a molecular weight of 22,000. The two types of subunits had similar amino acid compositions and showed amino-terminal sequence homology in 15 of 21 amino acids. The amino-terminal amino acid sequences of the B. pertussis fimbriae were distinct from those reported for fimbriae from other gram-negative bacteria. Neither the type 6 nor the type 2 fimbriae caused hemagglutination when assayed with several types of erythrocytes.

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae

Cowell¹,

Zhang²,

Urisu³

et al. 1987

Infect Immun

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“…Agglftinogen serotping. B. pertussis strains were serotyped by the microagglutination assay (19a) using typing sera prepared by G. Eldehng (11,12).…”

Section: Methodsmentioning

confidence: 99%

Filamentous hemagglutinin has a major role in mediating adherence of Bordetella pertussis to human WiDr cells

Urisu¹,

Cowell²,

Manclark³

1986

Infect Immun

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35S]methionine-labeled Bordetella pertussis adhered to monolayers of WiDr cells, an epitheliumlike cell line from a humah intestinal carcinoma. Adherence was proportional to the density of the WiDr cells and to the concentration of B. pertussis in the assay. Adherence of virulent phase I strains Tohama phase I, 114, and BP338 was much greater than adherence of avirtilent strains Tohama phase Ill and 423 phase IV. Muta,nts deficient in the production of the filamentous hemaggilitinin (FHA) were hemagglutination negative and adhered to WiDr cells much less efficiently than the parent strains. Preincubation of B. pertussis cells with FHA increased their hemagglutination activity and adherence to WiDr cells. Goat antibody to FHA inhibited, in a dbse-dependent manner, the adherence of strain Tohama I but not the adherence of FHA-deficient mutant Tohaina 325. At similar protein concentrations, normnal goat antibody, goat antibody to-pertussis toxin, or the Fab fragments of goat antibody to serotype 2 fimbriae had nb effect on adherence. Also, an FHA-positive strain withoit fimbriae showed high adherence, while a fimbriated FHA-defident mutant adhered poorly. Our data indicate that FHA plays a major role in adherence ofB. pertussis to human WilDr cells. Fimbriae do not appear to mediate attachment of B. pertussis to WiDr cells.

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“…Mice were immunized with the affinity-purified 69-kDa material, and the polyclonal antiserum obtained was tested 1 2 3 4 5…”

Section: Resultsmentioning

confidence: 99%

“…Andersen first identified five distinct agglutinogen factors (1), and subsequently Eldering et al added agglutinogen factor 6 (6). The U.S. Reference Factor 1 to 6 antisera prepared by Eldering et al (6) and three monospecific polyclonal antisera (Factors 1 to 3) produced by Preston (23) have been used to identify the serotypes of human isolates and to distinguish B. pertussis from the closely related species B. bronchiseptica and B. parapertussis (5,14,25). The prevalence of certain serotypes following outbreaks of whooping cough has been noted (8,25), and there is some evidence that serum agglutinin titers of human vaccinees correlate with clinical protection from pertussis (16).…”

mentioning

confidence: 99%

Identification of a 69-kilodalton nonfimbrial protein as an agglutinogen of Bordetella pertussis

et al. 1988

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Cells of Bordetella pertussis BP353, a nonfimbriated Eldering serotype 1.3 strain, were used as an immunogen to produce three monoclonal antibodies, BPE3, BPD8, and BPE8, that agglutinated the immunizing cells, as well as certain other nonfimbriated and fimbriated serotype 3-containing B. pertussis strains. The antibodies did not agglutinate serotype 1 or nontypable B. pertussis cells. These monoclonal antibodies specifically detected a 69-kilodalton (kDa) band on Western blots (immunoblots) containing whole B. pertussis cell lysates of Eldering agglutinogen serotypes 1.3, 1.3.6, 1.2.3.4, and 1.2.3.4.6. This 69-kDa antigen was released from the bacteria by cell incubation for 60 min at 60°C, and it was purified by affinity chromatography with a BPE3-agarose affinity matrix. Purified material was used to produce a polyclonal antiserum that agglutinated all nonfimbriated and fimbriated B. pertussis cells containing serotype 3 agglutinogen. Immunogold electron microscopy and indirect immunofluorescence studies demonstrated that it is an outer membrane constituent but nonfimbrial in appearance. BPE3 did not detect purified fimbriae on Western blots, and antibodies to these fimbriae did not bind to the 69-kDa component. Although B. bronchiseptica and B. parapertussis cells were not agglutinated by the monoclonal antibodies, antigenically similar proteins were detected in extracts of the bacteria. These results identify the 69-kDa protein as a nonfimbrial agglutinogen present on all virulent strains of B. pertussis. The monoclonal antibodies described here should be useful for further studies on the structure and function of this protein.

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Bordetella pertussis Serotypes in the United States

Cited by 18 publications

References 6 publications

Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae

Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae

Filamentous hemagglutinin has a major role in mediating adherence of Bordetella pertussis to human WiDr cells

Identification of a 69-kilodalton nonfimbrial protein as an agglutinogen of Bordetella pertussis

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