Dec 01, 2012 - MONMOUTH JUNCTION, NJ.– Authors Thierry Kamtchoua et al published an article in the journal Vaccine titled, ‘Safety and immunogenicity of the pneumococcal pneumolysin derivative PlyD1 in a single-antigen protein vaccine candidate in adults’ describing the immunogenicity of pneumococcal single antigen protein vaccine in a phase 1, randomized, placebo controlled dose escalating study. Authors cite Cleanascite™ from Biotech Support Group for removal of cholesterol from serum. A toxin neutralizing assay with antibodies in sera was developed to neutralize cytotoxicity caused by Ply in Vero cells. An incubated challenge dose of pneumolysin toxin containing serum diluted with or without Cleanascite™ was developed. The neutralizing titer inhibited the toxin’s effect on Vero cells. According to the paper, “Briefly, the toxin-neutralizing antibody titer was determined by incubating a challenge dose of pneumolysin toxin with serial 2-fold dilutions of serum treated with or without Cleanascite™ HC (Biotech Support Group) to remove cholesterol, an inhibitor of Ply”.
http://www.sciencedirect.com/science/article/pii/S0264410...
Characteristics Of Cleanascite™
Does not bind to DNA, RNA, enzymes and proteins
Leaves glycoproteins, antibodies, nucleic acids, hemoglobin, proteoglycans, nucleic acids, serum components(such as hormones, nutrients, globulins, clotting factors, transport proteins) alone
Extends the life of membrane and chromatographic columns.
Ideal for delipidation treatments for downstream processing of large-scale therapeutic proteins, enzymes and monclonal antibodies.
Ideal for clarifying ascites, serum, cell & tissue culture, bile and organ homogenates
For more information, visit:
Cleanascite™ Lipid Removal Reagent and Clarification
http://www.biotechsupportgroup.com/node/73
About Biotech Support Group LLC
Biotech Support Group LLC is a leading provider of genomics and proteomics sample preparation products and enrichment reagent kits as well as integrated biotechnology services for life sciences research, biomarker and drug discovery. Based in New Jersey, it’s principal products include: AlbuVoid™ for albumin depletion, Cleanascite™ for lipid adsorption and clarification, NuGel™ for passivated silica-based affinity chromatography, and ProCipitate™ & ProPrep™ for nucleic acid isolation. Currently, Biotech Support Group LLC and ProFACT Proteomics Inc., are collaborating on the development of a proteomics platform used in functional profiling for proteomic analysis and a separations method for generating sub-proteomes used in biomarker and functional proteomic prospecting. For more information, go to: www.biotechsupportgroup.com
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Cleanascite™ References
Plasma/Serum
Kamtchoua, Thierry, Monica Bologa, Robert Hopfer, David Neveu, Branda Hu, Xiaohua Sheng, Nicolas Corde, Catherine Pouzet, Gloria Zimmerman, and Sanjay Gurunathan. “Safety and immunogenicity of the pneumococcal pneumolysin derivative PlyD1 in a single-antigen protein vaccine candidate in adults.” Vaccine (2012). http://www.sciencedirect.com/science/article/pii/S0264410X12015988
Lijowski M, Caruthers S, Hu G. High-Resolution SPECT-CT/MR Molecular Imaging of Angiogenesis in the Vx2 Model Investigative Radiology.2009;44(1): 15–22
Turner JD, Langley RS, Johnston KL. Wolbachia Lipoprotein Stimulates Innate and Adaptive Immunity through Toll-like Receptors 2 and 6 to Induce Disease Manifestations of Filariasis The Journal of Biological Chemistry.2009;284:22364-22378
http://www.jbc.org/content/284/33/22364.full
Torrelles JB, DesJardin LE, MacNeil J. et al Inactivation of Mycobacterium tuberculosis mannosyltransferase pimB reduces the cell wall lipoarabinomannan and lipomannan content and increases the rate of bacterial-induced human macrophage cell death Glycobiology.2009;19(7):743-755
http://glycob.oxfordjournals.org/content/19/7/743.short
Cho N, Chueh PJ, Kim C et al Monoclonal antibody to a cancer-specific and drug-responsive hydroquinone (NADH) oxidase from the sera of cancer patients. Cancer Immunology, Immunotherapy. 2002;51(3):121-9 http://www.springerlink.com/content/92rtvqc5r1hafjfn/
Shapiro S, Beenhouwer DO, Feldmesser M et al. Immunoglobulin G Monoclonal Antibodies to Cryptococcus neoformans Protect Mice Deficient in Complement Component C3 Infect. Infection and immunity.2002;70(5):2598-604 http://iai.asm.org/cgi/content/abstract/70/5/2598
Castro AR, Morrill We, Pope V. Lipid Removal from Human Serum Samples Clinical and diagnostic laboratory immunology.2000;7(2):197-199 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC95848/
Nussbaum G, Cleare W, Casadevall A et al Epitope Location in the Cryptococcus neoformans Capsule Is a Determinant of Antibody Efficacy The Journal of experimental medicine.1997;185:685-694 http://jem.rupress.org/content/185/4/685.abstract
Suggested References
Salha, Danielle, et al. “Neutralizing Antibodies Elicited by a Novel Detoxified Pneumolysin Derivative, PlyD1, Provide Protection against Both Pneumococcal Infection and Lung Injury.” Infection and immunity 80.6 (2012): 2212-2220. http://iai.asm.org/content/80/6/2212.short
Pichichero, Michael E., et al. “Antibody response to Streptococcus pneumoniae proteins PhtD, LytB, PcpA, PhtE and Ply after nasopharyngeal colonization and acute otitis media in children.” Human Vaccines & Immunotherapeutics 8.6 (2012): 799-805. http://www.es.landesbioscience.com/journals/vaccines/article/19820/?show_full_text=true
Ljutic, Belma, et al. “Formulation, stability and immunogenicity of a trivalent pneumococcal protein vaccine formulated with aluminum salt adjuvants."Vaccine (2012). http://www.sciencedirect.com/science/article/pii/S0264410X12002320
Alexander, Janet E., et al. “Immunization of mice with pneumolysin toxoid confers a significant degree of protection against at least nine serotypes of Streptococcus pneumoniae.” Infection and immunity 62.12 (1994): 5683-5688. http://iai.asm.org/content/62/12/5683.short
Berry, A. M., J. Yother, D. E. Briles, D. Hansman, and J. C. Paton. “Reduced virulence of a defined pneumolysin-negative mutant of Streptococcus pneumoniae."Infection and immunity 57, no. 7 (1989): 2037-2042. http://iai.asm.org/content/57/7/2037.short
Tilley, Sarah J., et al. “Structural basis of pore formation by the bacterial toxin pneumolysin.” Cell 121.2 (2005): 247-256. http://www.sciencedirect.com/science/article/pii/S0092867405002321
Mitchell, T. J., et al. “Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein.” Molecular microbiology 5.8 (2006): 1883-1888. http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.1991.tb00812.x/abstract
Paton, James C. “The contribution of pneumolysin to the pathogenicity of Streptococcus pneumoniae.” Trends in microbiology 4, no. 3 (1996): 103-106. http://www.sciencedirect.com/science/article/pii/0966842X96815265
Boulnois, G. J., J. C. Paton, T. J. Mitchell, and P. W. Andrew. “Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae.” Molecular microbiology 5, no. 11 (1991): 2611-2616. http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.1991.tb01969.x/abstract
Nöllmann, Marcelo, et al. “The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin.” Biophysical journal 86.5 (2004): 3141-3151. http://www.sciencedirect.com/science/article/pii/S0006349504743623
