Chemical and immunochemical studies on the receptor binding domain of cholera toxin B subunit.
نویسندگان
چکیده
منابع مشابه
Designing, Optimization and Construction of Myelin Basic Protein Coding Sequence Binding to the Immunogenic Subunit of Cholera Toxin
Abstract Background and Objectives: Multiple sclerosis (MS) is a chronic inflammatory autoimmune disease. Mucosal feeding of myelin basic protein binding to the cholera toxin B subunit can reduce the intensity of the immune response in MS patients. Expression system, the domain composition of the fusion protein, accessibility of two domains, codon adaptation index (CAI) and GC contents are v...
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Background and Objective: Shiga toxin (STx) is the main virulence factor in Shigella Dysenteriae type I and is composed of an enzymatic subunit STxA monomer and a receptor-binding STxB homopentamer. Shigella toxin B subunit (STxB) is a non-toxic homopentameric protein responsible for toxin binding and internalization into target cells by interacting with glycolipid (Gb3). Cholera toxi...
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We increase our understanding of augmenting a cellular immune response, by using an HIV-1 protease-derived epitope (PR75-84), and variants thereof, coupled to the C-terminal, of the B subunit of cholera toxin (CTB). Fusion proteins were used for immunizations of HLA-A0201 transgenic C57BL/6 mice. We observed different capacities to elicit a cellular immune response by peptides with additions of...
متن کاملFusions to the cholera toxin B subunit: influence on pentamerization and GM1 binding.
The cholera toxin B (CTB) subunit has been used extensively in vaccine research as a carrier for peptide immunogens due to its immunopotentiating properties, where coupling has been obtained either by genetic fusion or chemical conjugation. For genetically fused immunogens both N- and C-terminal fusions have been used. Only shorter extensions have previously been evaluated and in some reports t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)38903-2