Lymphocytosis-promoting factor of Bordetella pertussis alters mononuclear phagocyte circulation and response to inflammation

Meade, Bruce D.; Kind, Phyllis D.; Manclark, C R

doi:10.1128/iai.46.3.733-739.1984

Cited by 40 publications

(14 citation statements)

References 36 publications

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“…PTX, in concert with FHA, is believed to be important in the adherence of B. pertussis to ciliated respiratory epithelial cells (63,64); thus, antibodies to PTX in respiratory secretions may protect by blocking bacterial adherence. It has also been postulated that PTX contributes to the persistence of the pulmonary infection by impairing the function of immune effector cells (27,68). PTX has been shown to inhibit the migration of mononuclear phagocytes (26,27) and to alter normal lymphocyte circulation (58).…”

Section: Discussionmentioning

confidence: 99%

Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen

et al. 1990

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Bordetella pertussis TOX3201 has a 12-base-pair insertion in the Si subunit gene of pertussis toxin (PTX), which encodes for a 4-amino-acid insertion between residues 107 and 108 of the mature S1 subunit (Black et al., Science 240:656-659, 1988). This mutant strain has been shown to secrete a holotoxin analog of PTX, designated CRM3201, with reduced ADP-ribosyltransferase activity. In the present study, we evaluated the biochemical, biological, and immunoprotective activities of purified CRM3201. Assay of enzymatic activities showed that CRM3201 had 20 to 30% of the ADP-ribosyltransferase activity and 55 to 60% of the NAD glycohydrolase activity of native PIX. CRM3201, however, had only 2 to 6% of the activity of PTX in clustering CHO cells, promoting leukocytosis, inducing histamine sensitization, and potentiating an anaphylactic response to bovine serum albumin. In contrast, activities associated with the B oligomer (binding to fetuin, hemagglutination of goose erythrocytes, and lymphocyte mitogen activity) were comparable to those of native PTX. Injection of BALB/c mice with CRM3201 mixed with Al(OH)3 elicited high titers of antibody to PTX (as measured by enzyme-linked immunosorbent assay), which neutralized a leukocytosis-promoting dose of PTX in these mice and neutralized PTX in a CHO cell assay. Passive transfer of the anti-CRM3201 antibody protected 20-day-old Swiss-Webster mice against a lethal aerosol challenge with B. pertussis 18323. Active immunization with CRM3201 significantly reduced lung colonization in adult BALB/c mice with a B. pertussis

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Section: Discussionmentioning

confidence: 99%

Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen

et al. 1990

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“…The molecular basis for the characteristic paroxysmal cough is not known, but is not mimicked by intravenous PT [41]. One likely role of PT is to impair the innate immune response of the host, causing leukolymphocytosis and blocking the migration of murine macrophages [42]. Reduced expression of l-selectin on the surface of leukocytes from infants infected with B. pertussis has also been demonstrated [43,44].…”

Section: Pathogenesis and Immunity In Pertussismentioning

confidence: 99%

International Bordetella pertussis assay standardization and harmonization meeting report. Centers for Disease Control and Prevention, Atlanta, Georgia, United States, 19–20 July 2007

Tondella

Carlone

Messonnier

et al. 2009

Vaccine

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An international meeting on Bordetella pertussis assay standardization and harmonization was held at the Centers for Disease Control and Prevention (CDC), Atlanta, GA, 19-20 July 2007. The goal of the meeting was to harmonize the immunoassays used for pertussis diagnostics and vaccine evaluation, as agreed upon by academic and government researchers, regulatory authorities, vaccine manufacturers, and the World Health Organization (WHO). The primary objectives were (1) to provide epidemiologic, laboratory, and statistical background for support of global harmonization; (2) to overview the current status of global epidemiology, pathogenesis and immunology of pertussis; (3) to develop a consensus opinion on existing gaps in understanding standardization of pertussis assays used for serodiagnosis and vaccine evaluation; and (4) to search for a multicenter process for addressing these priority gaps. Presentations and discussions by content experts addressed these objectives. A prioritized list of action items to improve standardization and harmonization of pertussis assays was identified during a group discussion at the end of the meeting. The major items included: (1) to identify a group that will organize, prepare, maintain, and distribute proficiency panels and key reagents such as reference and control sera; (2) to encourage the development and identification of one or more reference laboratories that can serve as an anchor and resource for other laboratories; (3) to define a performance-based assay method that can serve as a reference point for evaluating laboratory differences; (4) to develop guidance on quality of other reagents, e.g., pertussis toxin and other antigens, and methods to demonstrate their suitability; (5) to establish an international working group to harmonize the criteria to evaluate the results obtained on reference and proficiency panel sera; (6) to create an inventory to determine the amount of appropriate and well-characterized sera that are available globally to be used as bridging reagents for vaccine licensure; and (7) to seek specific guidance from regulatory authorities regarding the expectations and requirements for the licensure of new multicomponent pertussis vaccines.

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“…Pertussis toxin, an exotoxin produced by the organism Bordetella pertussis, displays a wide variety of biological effects, including the ability to induce leukocytosis, alter the host immune system and affect glucose homeostasis (25)(26)(27)35). These actions of the toxin result from its ability to bind to cells and subsequently ADP-ribosylate a family of GTPbinding regulatory proteins (G proteins) involved in hormonal signal transduction (6,16,19,20).…”

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confidence: 99%

Binding of pertussis toxin to eucaryotic cells and glycoproteins

et al. 1989

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The binding of pertussis toxin and its subunits to cell surface receptors and purified glycoproteins was examined. The interaction of pertussis toxin with components of two variant Chinese hamster ovary (CHO) cell lines was studied. These cell lines are deficient in either sialic acid residues (LEC 2) or sialic acid and galactose residues (LEC 8) on cell surface macromolecules. The binding of pertussis toxin to components of these cells differed from the binding of the toxin to wild-type components. Although the toxin bound to a 165,000-dalton glycoprotein found in N-octylglucoside extracts of wild-type cells, it did not bind to components found in extracts of LEC 2 cells. In contrast, the toxin bound to components found in extracts of LEC 8 cells, which are variant cells that contain increased amounts of terminal N-acetylglucosamine residues on cell surface macromolecules. These results suggest that the receptor for pertussis toxin on CHO cells contains terminal acetamido-containing sugars. The cytopathic effect of the toxin on both types of variant cells was much reduced compared with its effects on wild-type cells. Thus, optimal functional binding of pertussis toxin appears to require a complete sialyllactosamine (NeuAc-+GalPi4GlcNAc) sequence on surface macromolecules. In

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Lymphocytosis-promoting factor of Bordetella pertussis alters mononuclear phagocyte circulation and response to inflammation

Cited by 40 publications

References 36 publications

Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen

Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen

International Bordetella pertussis assay standardization and harmonization meeting report. Centers for Disease Control and Prevention, Atlanta, Georgia, United States, 19–20 July 2007

Binding of pertussis toxin to eucaryotic cells and glycoproteins

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