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T Sklaviadis - One of the best experts on this subject based on the ideXlab platform.
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Antigenic profile of human recombinant PrP: generation and characterization of a versatile Polyclonal Antiserum.
Journal of neuroimmunology, 2004Co-Authors: M Sachsamanoglou, I Paspaltsis, S Petrakis, S Verghese-nikolakaki, C H Panagiotidis, T Voigtlander, H Budka, J P M Langeveld, T SklaviadisAbstract:We describe the quality of a rabbit Polyclonal Antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 Antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the Antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen.Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge.
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Antigenic profile of human recombinant PrP: generation and characterization of a versatile Polyclonal Antiserum
Journal of Neuroimmunology, 2003Co-Authors: M Sachsamanoglou, I Paspaltsis, S Petrakis, S Verghese-nikolakaki, C H Panagiotidis, T Voigtlander, H Budka, J Langeveld, T SklaviadisAbstract:We describe the quality of a rabbit Polyclonal Antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 Antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the Antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen. Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge. D 2003 Elsevier B.V. All rights reserved.
M Sachsamanoglou - One of the best experts on this subject based on the ideXlab platform.
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Antigenic profile of human recombinant PrP: generation and characterization of a versatile Polyclonal Antiserum.
Journal of neuroimmunology, 2004Co-Authors: M Sachsamanoglou, I Paspaltsis, S Petrakis, S Verghese-nikolakaki, C H Panagiotidis, T Voigtlander, H Budka, J P M Langeveld, T SklaviadisAbstract:We describe the quality of a rabbit Polyclonal Antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 Antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the Antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen.Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge.
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Antigenic profile of human recombinant PrP: generation and characterization of a versatile Polyclonal Antiserum
Journal of Neuroimmunology, 2003Co-Authors: M Sachsamanoglou, I Paspaltsis, S Petrakis, S Verghese-nikolakaki, C H Panagiotidis, T Voigtlander, H Budka, J Langeveld, T SklaviadisAbstract:We describe the quality of a rabbit Polyclonal Antiserum (Sal1) that was raised against mature human recombinant prion protein (rhuPrP). Epitope mapping demonstrated that the Sal1 Antiserum recognized six to eight linear antigenic sites, depending on the animal species. The versatility of the Antiserum was evident from the range of animal species and immunochemical techniques where it could be applied successfully. Antigen absorption studies revealed differences in the location and number of epitopes remaining after incubation with soluble or aggregated antigen. Our knowledge concerning immunoprophylaxis against prion diseases and the important role played by conformational changes of PrP is increasing rapidly. The findings reported here should add to this body of knowledge. D 2003 Elsevier B.V. All rights reserved.
M. B. Kerrn - One of the best experts on this subject based on the ideXlab platform.
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Test of a Novel Streptococcus pneumoniae Serotype 6C Type Specific Polyclonal Antiserum (Factor Antiserum 6d) and Characterisation of Serotype 6C Isolates in Denmark
BMC infectious diseases, 2010Co-Authors: Lotte Lambertsen, M. B. KerrnAbstract:Background: In 2007, Park et al. identified a novel serotype among Streptococcus pneumoniae serogroup 6 which they named serotype 6C. The aim of this study was to evaluate with the Neufeld test a novel S. pneumoniae serotype 6C type specific Polyclonal Antiserum. In addition, serotype 6C isolates found in Denmark in 2007 and 2008 as well as eight old original serotype 6A isolates were characterised. Methods: In this study, 181 clinical Streptococcus pneumoniae isolates from Denmark 2007 and 2008 were examined; 96 isolates had previously been typed as serotype 6A and 85 as serotype 6B. In addition, eight older isolates from 1952 to 1987, earlier serotyped as 6A, were examined. Serotype 6C isolates were identified by PCR and serotyping with the Neufeld test using the novel type specific Polyclonal Antiserum, factor Antiserum 6 d, in addition to factor antisera 6b, 6b* (absorbed free for cross-reactions to serotype 6C) and 6c. All antisera are commercially available and Antiserum 6b obtained from the supplier after 1 January 2009 is Antiserum 6b*. All serotype 6C isolates were further characterised using multi-locus sequence typing. Results: When retesting all 96 original serotype 6A isolates by PCR and the Neufeld test, 29.6% (24 of 81) of the invasive isolates in Denmark from 2007 and 2008 were recognised as serotype 6C. In addition, three of eight old isolates originally serotyped as 6A were identified to be serotype 6C. The oldest serotype 6C isolate was from 1962. The serotype 6C isolates belonged to eleven different sequence types (ST) and nine clonal complexes (CC), ST1692 (CC395), ST386 (CC386) and ST481 (CC460) were the predominant types. Conclusions: We tested a novel Polyclonal Antiserum 6 d, as well as modified Antiserum 6b*, provided a scheme for the serotyping of S. pneumoniae serogroup 6 using the Neufeld test and compared the serotyping method with PCR based methods. The two types of methods provided the same results. In future, it will, therefore, be possible to test also serotype 6C in accordance to the standard method for serotyping of S. pneumoniae recommended by WHO. Among all invasive isolates from Denmark 2007 and 2008, serotype 6C constituted 29.6% of the original serotype 6A isolates. The serotype 6C isolates were found to be diverse belonging to a number of different STs and CCs of which most have been observed in other countries previously. Serotype 6C is regarded as an “old” serotype being present among S. pneumoniae isolates in Denmark for at least 48 years. The genetic diversity of serotype 6C isolates and their genetic relationship to other serotypes suggested that serotype 6C strains may have arisen from several different independent recombination events involving different parental strains such as serotypes 6A, 6B, 23F and 4.
P. L. Guy - One of the best experts on this subject based on the ideXlab platform.
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An improved Polyclonal Antiserum for detecting Ryegrass mosaic rymovirus.
Archives of virology, 2005Co-Authors: D. E. Webster, D. L. Beck, F. Rabenstein, Richard L S Forster, P. L. GuyAbstract:Ryegrass mosaic virus (RGMV) is considered the most serious and widespread virus infecting temperate pasture grasses. The use of visible symptoms to diagnose infection is unreliable and ELISA analysis requires antibodies with broad cross-reactivity. Here we describe the production of a Polyclonal Antiserum (PAb-cp3′Δ) using a bacterially expressed RGMV coat protein fragment. The PAb-cp3′Δ Antiserum is specific for RGMV and recognises RGMV strains from each major phylogenetic cluster. PAb-cp3′Δ may be used in ELISAs for fast, accurate and inexpensive detection of RGMV.
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An improved Polyclonal Antiserum for detecting Ryegrass mosaic rymovirus Brief Report
2005Co-Authors: D. E. Webster, D. L. Beck, F. Rabenstein, Richard L S Forster, P. L. GuyAbstract:Ryegrass mosaic virus (RGMV) is considered the most serious and widespread virus infecting temperate pasture grasses. The use of visible symptoms to diagnose infection is unreliable and ELISA analysis requires antibodies with broad cross-reactivity. Here we describe the production of a Polyclonal Antiserum (PAb-cp3′∆) using a bacterially expressed RGMV coat protein fragment. The PAb-cp3′∆ Antiserum is specific for RGMV and recognises RGMV strains from each major phylogenetic cluster. PAb-cp3′∆ may be used in ELISAs for fast, accurate and inexpensive detection of RGMV. ∗
Ramadan A. Abuknesha - One of the best experts on this subject based on the ideXlab platform.
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Enzyme immunoassays for the analysis of streptomycin in milk, serum and water: development and assessment of a Polyclonal Antiserum and assay procedures using novel streptomycin derivatives.
The Analyst, 2005Co-Authors: Ramadan A. Abuknesha, Connie LukAbstract:A Polyclonal Antiserum to streptomycin was generated in sheep using a streptomycin-bovine serum albumin conjugate as immunogen. Streptomycin was linked to the carrier protein with cyanuric chloride using a new two-step conjugation method. Plate coating antigen conjugates of streptomycin and gelatine were prepared using either cyanuric chloride (homologous bridge) or 1,4-butanediol diglycidyl ether to provide an heterologous complex. The reagents enabled the generation of a specific Antiserum with a titre of 1/40,000 and the development of a sensitive ELISA method suitable for the measurement of streptomycin sulfate in milk, serum and water samples. A minimum detection value of 1 ng mL−1 and a dynamic range of 1 to 200 ng mL−1 were demonstrated in the three matrices. No detectable cross reactivity with any of the common aminoglycosides was found except the related dihydrostreptomycin which gave a 75% cross reaction value. The details of the preparation of the hapten–protein conjugates, characterisation of the Antiserum and assay construction and assessment methods are presented. The introduction of new coupling methods and antibody assessment provide improved basic methodologies necessary for the advancement of immuno-analysis of streptomycin, one of the most widely used antimicrobial substances.
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Evaluation of a Polyclonal Antiserum to pentachlorothiophenol-acetic acid-KLH immunogen: binding properties and use with heterologous PCP derivatives in ELISA for pentachlorophenol
Analytical and bioanalytical chemistry, 2004Co-Authors: Ramadan A. Abuknesha, Hannah M. T. GriffithAbstract:A Polyclonal Antiserum to pentachlorothiophenol-acetic acid-KLH was generated in sheep and assessed by solid phase ELISA. The assessment procedure included use of double checkerboard analysis in the absence and in the presence of analyte loads, estimation of cross reactivities of chlorophenol pesticides, assessment of the effect of pH, Tween 20, and Thames water matrix. The Antiserum was highly specific for pentachlorophenol and enabled minimum detection limits of less than 0.2 ng mL−1 in river water matrix. Particularly important was the significant improvement of assay performance in the absence of Tween 20 and at pH 4 and the very low cross reactivity (less than 0.01%) for other commonly used chlorophenols—2,4,5-trichlorophenol and 2,4,6-trichlorophenol, 2-methyl-4-chlorophenoxyacetic acid, and 2,4-dichlorophenoxy acetic acid. The study re-affirms the importance of the judicious choice of hapten derivatives in the synthesis of immunogens and assay reagents for pentachlorophenol analysis by competitive immunoassays.