Effect of lymphocytosis-promoting factor from Bordetella pertussis on cerebellar cyclic GMP levels

Askelöf, Per; Gillenius, Pekka

doi:10.1128/iai.36.3.958-961.1982

Cited by 22 publications

(3 citation statements)

References 26 publications

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“…For their ELISA for PT antibody, Sato and co-workers (15) treated the wells with human haptoglobulin before sensitization with purified PT to increase antigen adsorption. In our study, we used F both as the immunosorbent for PT (1,17) and as an anchor of antigen to the ELISA wells. F-coated wells were used both as affinity columns for purifying PT and as reaction sites for serologic activity.…”

Section: Discussionmentioning

confidence: 99%

New, practical approach to detecting antibody to pertussis toxin for public health and clinical laboratories

Wong

Skelton

1988

J Clin Microbiol

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A new, practical method for determining antibody to pertussis toxin (PT) by enzyme-linked immunosorbent assay for public health and clinical laboratories is possible because of recent advances in understanding the pathobiology of Bordetella pertussis and the physicochemical properties of PT. The new approach does not require the use of highly purified PT antigen, whiçh is difficult and expensive for most laboratories to obtain. Moreover, it employs only reagents that are commercial readily available. The method combines the purification of PT antigen and an assay for PT antibody into one process. It depends on (i) growth ofB. pertussis in a simple, defined medium to obtain a PT-rich supernatant with little contamination of cellular antigens; (ià) a simple, one-step concentration of PT in the culture supernatant with Affi-Gel Blue (Bio-Rad Laboratories, Richmond, Calif.); and (iii) specific adsorption of PT as the test antigen to microtiter wells coated with fetuin for the enzyme-linked immunosorbent assay. The procedure is sensitive and specific for PT antibody. It is technically simple, reproducible, and can be performed in a modestly equipped laboratory.

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Section: Discussionmentioning

confidence: 99%

New, practical approach to detecting antibody to pertussis toxin for public health and clinical laboratories

Wong

Skelton

1988

J Clin Microbiol

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“…(The use of haptoglobin was based on the empiric observation that pertussis toxin agglutinates erythrocytes with high sialic acid content on their surface [especially goose erythrocytes]. The sialic acid content of haptoglobin appears to be the basis of its specificity, because other sialic acid-rich proteins, such as fetuin, also serve as effective affinity ligands [1].) The hydroxylapatite eluate was passed over the 35-ml hemoglobin-haptoglobin column.…”

mentioning

confidence: 99%

Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin

Hewlett¹,

Sauer²,

Myers³

et al. 1983

Infect Immun

242

126

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Exposing Chinese hamster ovary cells in culture to pertussis toxin resulted in a novel clustered growth pattern. The specificity of the response for pertussis toxin was shown by neutralization of the activity with specific anti-toxin antibody, heat lability (80°C for 15 min), and absence of such activity by culture media from nontoxigenic Bordetella species. Although a lag of at least 16 h was required

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“…Phase I strains of Bordetella pertussis produce two distinct hemagglutinins (3, 15,16). The lymphocytosis-promoting factor hemagglutinin (LPF) appears as spherical structures 6 nm in diameter by electron microscopy (4,15,22), has a relatively low hemagglutinating activity, and induces a variety of biological responses, including leukocytosis and lymphocytosis, histamine sensitization, lethality, mitogenicity, adjuvant effects, and potentiation of insulin secretion (3,15,16,22,24). Munoz and Bergman refer to LPF as pertussigen (26), and it is now clear, based on biological activities (24), antigenic properties (7,21), and chemical and physical properties (15,16,22) that LPF is also identical to the islet-activating protein also isolated from B. pertussis (32,33).…”

mentioning

confidence: 99%

Separation and purification of the hemagglutinins from Bordetella pertussis

Sato¹,

Cowell²,

Sato³

et al. 1983

Infect Immun

121

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The role of the filamentous hemagglutinin (FHA) and the lymphocytosis-promoting factor hemagglutinin (LPF) in pertussis pathogenesis and immunity is the subject of active investigation. To be certain of their role as protective antigens, the hemagglutinins must be pure and free of each other. This report describes procedures to separate and purify FHA and LPF from the culture supernatant of stationary cultures of Bordetella pertussis Tohama, using hydroxylapatite, haptoglobin-Sepharose, and Sepharose CL-6B filtration chromatography. Purified FHA contained less than 0.002% active LPF assayed by histamine-sensitizing activity, and both hemagglutinins contained less than 0.01% of each other based on antigenic activity measured by an enzyme-linked immunosorbent assay, using affinity chromatography-purified antibody to each hemagglutinin. LPF and FHA were also shown to be antigenically distinct by immunodiffusion and were judged to be highly purified proteins by polyacrylamide gel electrophoresis. In addition, the purification procedures yielded milligram amounts of each hemagglutinin with very good recovery of starting activities.

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Effect of lymphocytosis-promoting factor from Bordetella pertussis on cerebellar cyclic GMP levels

Cited by 22 publications

References 26 publications

New, practical approach to detecting antibody to pertussis toxin for public health and clinical laboratories

New, practical approach to detecting antibody to pertussis toxin for public health and clinical laboratories

Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin

Separation and purification of the hemagglutinins from Bordetella pertussis

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