Production of anti-idiotypic monoclonal antibodies that mimic the phytotoxin dothistromin

• Published in: Food and agricultural immunology Vol. 10; no. 1; pp. 67 - 78
• Main Authors: Jones, William T., Harvey, Dawn, Sutherland, Paul W., Reynolds, Paul H. S.
• Format: Journal Article
• Language: English
• Published: London Taylor & Francis Group 01-03-1998; Taylor and Francis
• Subjects: Agronomy. Soil science and plant productions; anti-idiotypic mimic; Biological and medical sciences; Biotechnology; Dothistromin; ELISA; Fundamental and applied biological sciences. Psychology; Fungal plant pathogens; Generalities. Techniques; Genetics and breeding of economic plants; monoclonal antibodies; Pest resistance; Phytopathology. Animal pests. Plant and forest protection; Plant pathogens; Varietal selection. Specialized plant breeding, plant breeding aims; Plant pathology; Embryo; Plant pathogen; Binding site; Monoclonal antibody; Pinus radiata; Fungi; Softwood forest tree; Gymnospermae; Production; Fungi Imperfecti; Ungulata; Thallophyta; Method study; Bovine; Phytotoxin; Dothistroma pini; Mimic; Mycology; Rodentia; Serum albumin; Experimental study; Fungus resistance; Biological compound; Screening; Vertebrata; Mammalia; Analysis method; Mouse; Preparation; Genetic improvement; Forestry; Antiidiotypic antibody; Coniferales; Spermatophyta; Artiodactyla; ELISA assay; dothistromin
• ISSN: 0954-0105; 1465-3443
• DOI: 10.1080/09540109809354970

Dothistromin (DOTH) is a toxin secreted by Dothistroma pini and is present in needle lesions resulting from infection by this fungus. A monoclonal antibody (MAb 10C12) of high affinity for DOTH was conjugated to bovine serum albumin (BSA) and used to immunize mice in order to prepare monoclonal anti-idiotypic antibody mimics of dothistromin. One anti-idiotypic antibody, 12C9G8, was equivalent to DOTH on a molar basis in inhibition of the binding of an anti-DOTH MAb to DOTH-protein conjugates. Furthermore, in a Western blot analysis, 12C9G8 visualized the same protein profile in embryos as was observed in an approach which utilized an anti-DOTH MAb together with DOTH-mouse serum albumin (MSA) conjugate to identify potential DOTH binding sites. In a parallel immunogold electron microscopy experiment, protein-containing vesicles were labelled using both approaches.