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Search results for: Anti-Bordetella pertussis Purified Preparations Antibody

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#31036455   2019/04/26 To Up

Proteomics of diphtheria toxoid vaccines reveals multiple proteins that are immunogenic and may contribute to protection of humans against Corynebacterium diphtheriae.

Introduced for mass immunization in the 1920s, vaccines against diphtheria are among the oldest and safest vaccines known. The basic principle of their production is the inactivation of purified diphtheria toxin by formaldehyde cross-linking, which converts the potentially fatal toxin in a completely harmless protein aggregate, which is still immunogenic. Since in addition to diphtheria toxin also other proteins may be secreted by Corynebacterium diphtheriae during cultivation, we assumed that diphtheria toxoid might not be the only component present in the vaccine. To address this question, we established a protocol to reverse formaldehyde cross-linking and carried out mass spectrometric analyses. Different secreted, membrane-associated and cytoplasmic proteins of C. diphtheriae were detected in several vaccine preparations from across the world. Based on these results, bioinformatics and Western blot analyses were applied to characterize if these proteins are immunogenic and may therefore support protection against C. diphtheriae. In frame of this study, we could show that the C. diphtheriae toxoid vaccines induce antibodies against different C. diphtheriae proteins and against diphtheria toxin secreted by Corynebacterium ulcerans, an emerging pathogen which is outnumbering C. diphtheriae as cause of diphtheria-like illness in Western Europe.
Jens Möller, Max Kraner, Uwe Sonnewald, Vartul Sangal, Hannes Tittlbach, Julia Winkler, Thomas H Winkler, Vyacheslav Melnikov, Roland Lang, Andreas Sing, Ana Luiza Mattos-Guaraldi, Andreas Burkovski

1908 related Products with: Proteomics of diphtheria toxoid vaccines reveals multiple proteins that are immunogenic and may contribute to protection of humans against Corynebacterium diphtheriae.

100 1 mL1 mL1 mL1 mL10100 1mg51 ml200 20

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#24738289   // To Up

[Immunobiological properties of Bordetella pertussis lipopolysaccharide in the acellular pertussis vaccine].

Study of Bordetella pertussis lipopolysaccharide (LPS) immunobiological properties in the acellular pertussis vaccine.
E M ZaÄ­tsev, A V Poddubikov, M V Britsina, N U Mertsalova, M N Ozeretskovskaia, I G Bazhanova, N G Plekhanova

1364 related Products with: [Immunobiological properties of Bordetella pertussis lipopolysaccharide in the acellular pertussis vaccine].

100μg100μg100μg25100μg1250.2 mg

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#22527330   2012/04/15 To Up

Bordetella Pertussis Toxin does not induce the release of pro-inflammatory cytokines in human whole blood.

Pertussis Toxin (PTx) is one of the most important virulence factors of Bordetella pertussis, the cause of whooping cough. Therefore, the inactivated toxin is an obligatory constituent of acellular pertussis vaccines. It is described in the literature that both native PTx and recombinant Pertussis Toxin (PTg) activate human monocytes whereas others report an inhibition of mammalian monocytes during pertussis infection. B. pertussis, as a Gram-negative bacterium, harbours naturally lipopolysaccharide (LPS, also known as endotoxin), one of the strongest stimulators of monocytes. The latter is triggered via the interaction of endotoxin with inter alia the surface receptor CD14. Consequently, it is necessary to consider a potential contamination of Pertussis Toxin preparations with LPS. First, we determined the LPS content in different preparations of PTx and PTg. All preparations examined were contaminated with LPS; therefore, possible PTx- and PTg-driven monocyte activation independently of LPS was investigated. To meet these aims, we examined monocyte response to PTx and PTg while blocking the LPS receptor CD14 with a specific monoclonal antibody (anti-CD14 mAb). In addition, all toxin preparations examined underwent an LPS depletion. Our results show that it is contaminating LPS, not Pertussis Toxin, which activates human monocytes. Blocking the CD14 receptor prevents Pertussis Toxin-mediated induction of pro-inflammatory cytokines in human monocytes. The depletion of LPS from Pertussis Toxin leads to the same effect. Additionally, the PTx toxicity after LPS depletion procedure was confirmed by animal tests. In contrast, the original Pertussis Toxin preparations not treated as mentioned above generate strong monocyte activation. The results in this publication allow the conclusion that purified Pertussis Toxin preparations do not induce the release of pro-inflammatory cytokines in human whole blood.
Christina Bache, Ingo Spreitzer, Bjoern Becker, Bettina Loeschner, Ute Rosskopf, Kay-Martin Hanschmann, Michael Schwanig, Christian K Schneider, Bernhard Lieb, Thomas Montag

1093 related Products with: Bordetella Pertussis Toxin does not induce the release of pro-inflammatory cytokines in human whole blood.

2ug5ug2ug5ug96 tests2ug5ug50 ul16 Arrays/Slide 100 UG 100ul16 Arrays/Slide

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#21782823   2011/07/18 To Up

EUVAC.NET collaborative study: evaluation and standardisation of serology for diagnosis of pertussis.

As part of the new EUVAC.NET contract with ECDC (Pertussis Work Area 4), a collaborative study was organised in July-December 2010. Two well-defined reference preparations with high and low IgG antibodies to pertussis toxin (PT), were sent to participants. The purposes of this study were to assess current laboratory performance of serological assays for pertussis; to compare in-house reference preparations that are currently used by participants for the serological assay; and to identify needs for standardisation of the serological assay. Reference Laboratories in Europe currently performing serological assays for the diagnosis of pertussis by measuring antibody to PT, were invited to participate in the study. A total of 17 laboratories/countries participated in this study. Results were reported from a total of 9 participants who used in-house ELISA assays and 10 participants who used commercial kits. All participants using in-house ELISA with purified PT coating plates distinguished the 2 preparations and gave results that were comparable to the expected values. A total of 6 commercial kits included in the study showed different results. The kits coated with mixture antigens did not appear to be able to give results that were correlated to the WHO reference preparations.
Dorothy Xing, Kevin Markey, Penny Newland, Peter Rigsby, Jason Hockley, Qiushui He

2119 related Products with: EUVAC.NET collaborative study: evaluation and standardisation of serology for diagnosis of pertussis.

5 G1 mg 5 G0.1 mg 100 G2100 assays2.5 mg100ul10 mg10 ml

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#20943873   2010/10/13 To Up

Performance of commercial enzyme-linked immunosorbent assays for detection of antibodies to Bordetella pertussis.

Measuring antibodies to Bordetella pertussis antigens is mostly done by enzyme-linked immunosorbent assays (ELISAs). We compared the performance of ELISA kits that were commercially available in Germany. Eleven measured IgG antibodies, and nine measured IgA antibodies. An in-house ELISA with purified antigens served as a reference method. Samples included two WHO reference preparations, the former Food and Drug Administration (FDA)/Center for Biologics Evaluation and Research (CBER) reference preparations, serum samples from patients with clinically suspected pertussis, and serum samples from patients having received a combined tetanus, diphtheria, and pertussis (Tdap) vaccination. Kits using pertussis toxin (PT) as an antigen showed linearity compared to the WHO Reference preparation (r2 between 0.82 and 0.99), and these kits could quantify antibodies according to the reference preparation. ELISA kits using mixed antigens showed no linear correlation to the reference preparations. Patient results were compared to results of in-house ELISAs using a dual cutoff of either ≥100 IU/ml anti-PT IgG or ≥40 IU/ml anti-PT IgG together with ≥12 IU/ml anti-PT IgA. The sensitivities of kits measuring IgG antibodies ranged between 0.84 and 1.00. The specificities of kits using PT as an antigen were between 0.81 and 0.93. The specificities of kits using mixed antigens were between 0.51 and 0.59 and were thus not acceptable. The sensitivities of kits measuring IgA antibodies ranged between 0.53 and 0.73, and the specificities were between 0.67 and 0.94, indicating that IgA antibodies may be of limited diagnostic value. Our data suggest that ELISAs should use purified PT as an antigen and be standardized to the 1st International Reference preparation.
M Riffelmann, K Thiel, J Schmetz, C H Wirsing von Koenig

2725 related Products with: Performance of commercial enzyme-linked immunosorbent assays for detection of antibodies to Bordetella pertussis.

0.2 mg100 μg1 mL1 mg200 ug100 1 mL0.5 ml

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#18602434   2008/07/03 To Up

European Sero-Epidemiology Network 2: standardisation of immunoassay results for pertussis requires homogeneity in the antigenic preparations.

A standardisation process, already developed during the earlier European Sero-Epidemiology Network (ESEN) project, was employed with a more robust algorithm to harmonise results of pertussis serological assays performed in 12 European and non-European countries. Initially, results from each country's own assay were compared with those obtained at the reference laboratory by means of an in-house pertussis toxin (PT)-based ELISA: seven countries used in-house or commercial PT-ELISAs; the other countries used assays based on Bordetella pertussis whole cell extracts (WCE) (three countries) or on combined PT-FHA (filamentous haemagglutinin) antigenic preparations (two countries). The WCE assays, although admitted for diagnostic purposes, confirmed their low correlation with the PT-ELISAs and their results could not be used for standardisation; the PT-FHA ELISAs gave results that were suitable for standardisation in one country but unsatisfactory in the other; the use of purified PT in serological assays confirmed its better reliability than other preparations and all PT-ELISAs results could be calibrated against those of the reference centre. In the standardisation process two high-titre cut-offs indicative of likelihood of recent infection (from within 4 weeks of disease onset up to 1 year after) were included for evaluations as they are suggested to be more useful, for the sero-epidemiological assays of immunity to pertussis, than the cut-off of protection, commonly employed, but still not defined for pertussis. Providing PT-ELISAs are used, standardisation of pertussis assay results is always possible and, when standardisation is performed, evaluation and comparison of the impact of different interventions can be also allowed, by measuring at the distribution of high antibody titres in the populations.
Anna Giammanco, Antony Nardone, Richard Pebody, George Kafatos, Nick Andrews, Alfredo Chiarini, Susanna Taormina, Fernando de Ory, Katarina Prosenc, Bohumir Krize, Hans Hallander, Margaretha Ljungman, Esther Marva, Athanassios Tsakris, Darina O'Flanagan, François Schneider, Algirdas Griskevicius, Robert Vranckx, Ildiko Karacs

1313 related Products with: European Sero-Epidemiology Network 2: standardisation of immunoassay results for pertussis requires homogeneity in the antigenic preparations.

1500 MG 100 G

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#14977963   // To Up

Adenylate cyclase toxin from Bordetella pertussis synergizes with lipopolysaccharide to promote innate interleukin-10 production and enhances the induction of Th2 and regulatory T cells.

Adenylate cyclase toxin (CyaA) from Bordetella pertussis can subvert host immune responses allowing bacterial colonization. Here we have examined its adjuvant and immunomodulatory properties and the possible contribution of lipopolysaccharide (LPS), known to be present in purified CyaA preparations. CyaA enhanced antigen-specific interleukin-5 (IL-5) and IL-10 production and immunoglobulin G1 antibodies to coadministered antigen in vivo. Antigen-specific CD4(+)-T-cell clones generated from mice immunized with antigen and CyaA had cytokine profiles characteristic of Th2 or type 1 regulatory T (Tr1) cells. Since innate immune cells direct the induction of T-cell subtypes, we examined the influence of CyaA on activation of dendritic cells (DC) and macrophages. CyaA significantly augmented LPS-induced IL-6 and IL-10 and inhibited LPS-driven tumor necrosis factor alpha and IL-12p70 production from bone marrow-derived DC and macrophages. CyaA also enhanced cell surface expression of CD80, CD86, and major histocompatibility class II on immature DC. The stimulatory activity of our CyaA preparation for IL-10 production and CD80, CD86, and major histocompatibility complex class II expression was attenuated following the addition of polymyxin B or with the use of DC from Toll-like receptor (TLR) 4-defective mice. However, treatment of DC with LPS alone at the concentration present in the CyaA preparation (0.2 ng/ml) failed to activate DC in vitro. Our findings demonstrate that activation of innate cells in vitro by CyaA is dependent on a second signal through a TLR and that CyaA can promote Th2/Tr1-cell responses by inhibiting IL-12 and promoting IL-10 production by DC and macrophages.
Pádraig J Ross, Ed C Lavelle, Kingston H G Mills, Aoife P Boyd

2216 related Products with: Adenylate cyclase toxin from Bordetella pertussis synergizes with lipopolysaccharide to promote innate interleukin-10 production and enhances the induction of Th2 and regulatory T cells.

1000 TESTS/0.65ml1000 tests1000 tests0.2 mg1000 tests1000 tests100ug100ug 100ul100μg1 mg0.2 mg

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#14532091   // To Up

Identification of peptides that mimic the pertussis toxin binding site on bovine fetuin.

The introduction of acellular pertussis vaccines has greatly enhanced the safety profile of vaccines to prevent whooping cough. Pertussis toxin (Ptx) is one component produced by Bordetella pertussis that is contained in all of these vaccines, either in combination with other known pertussis virulence factors or as the sole pertussis component, combined with tetanus and diphtheria toxoids. A hydrogen peroxide toxoid of Ptx has been shown to be efficacious in preventing pertussis infections in a mass vaccination trial and is presently licensed in the United States and Europe (B. Trollfors, J. Taranger, T. Lagergard, L. Lind, V. Sundh, G. Zackrisson, C. U. Lowe, W. Blackwelder, and J. B. Robbins, N. Engl. J. Med. 333:1045-1050, 1995). The industrial production of Ptx can be performed through the cultivation of B. pertussis in well-defined growth media, in which the components can be well characterized and their origins can be documented. Once the bacteria are removed from the culture, Ptx can be isolated from the supernatant and purified by using the technique described by Sekura et al. (R. D. Sekura, F. Fish, C. R. Manclark, B. Meade, and Y. L. Zhang, J. Biol. Chem. 258:14647-14651, 1983). The only drawback of this procedure, which combines two affinity chromatography steps, one with Blue Sepharose and a second with matrix-bound bovine fetuin (BF), is the source and purity of the BF. Concern about vaccine preparations that may possibly risk contamination by material associated with bovine spongioform encephalopathy has continued to increase. We thus sought a replacement for the BF affinity chromatography and, more specifically, for the glycosidic moiety on BF. We describe here the identification of a seven-amino-acid peptide that mimics the glycosidic moiety on BF to which Ptx binds. Furthermore, we have constructed an affinity column containing this peptide that can be used to replace BF in Ptx purification. Finally, we used the X-ray crystallographic structure of Ptx bound to the oligosaccharide moiety of BF as a scaffold and replaced the oligosaccharide with the peptide.
John A Bogdan, Wei Yuan, Karen O Long-Rowe, Jawad Sarwar, Eric Allen Brucker, M S Blake

2033 related Products with: Identification of peptides that mimic the pertussis toxin binding site on bovine fetuin.

0.2 mg1 mg0.2 mg25100g100ug Lyophilized100 30ml100.00 ug100ug

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