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Immunomodulation of enzyme function in plants by single-domain antibody fragments.
Jobling, Stephen A; Jarman, Carl; Teh, Min-Min; Holmberg, Niklas; Blake, Caroline; Verhoeyen, Martine E.
Affiliation
  • Jobling SA; Unilever R&D Colworth, Sharnbrook, Bedford MK44 1LQ, UK. Steve.Jobling@Joblinghome.Freeserve.co.uk
Nat Biotechnol ; 21(1): 77-80, 2003 Jan.
Article in En | MEDLINE | ID: mdl-12483224
ABSTRACT
Immunomodulation involves the use of antibodies to alter the function of molecules and is an emerging tool for manipulating both plant and animal systems. To realize the full potential of this technology, two major obstacles must be overcome. First, most antibodies do not function well intracellularly because critical disulfide bonds cannot form in the reducing environment of the cytoplasm or because of difficulties in targeting to subcellular organelles. Second, few antibodies bind to the active sites of enzymes and thus they generally do not neutralize enzyme function. Here we show that the unique properties of single-domain antibodies from camelids (camels and llamas) can circumvent both these obstacles. We demonstrate that these antibodies can be correctly targeted to subcellular organelles and inhibit enzyme function in plants more efficiently than antisense approaches. The use of these single-domain antibody fragments may greatly facilitate the successful immunomodulation of metabolic pathways in many organisms.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Starch / Solanum tuberosum / Adjuvants, Immunologic / Immunoglobulin Heavy Chains / 1,4-alpha-Glucan Branching Enzyme Type of study: Evaluation_studies Limits: Animals Language: En Journal: Nat Biotechnol Journal subject: BIOTECNOLOGIA Year: 2003 Document type: Article Affiliation country:
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Collection: 01-internacional Database: MEDLINE Main subject: Starch / Solanum tuberosum / Adjuvants, Immunologic / Immunoglobulin Heavy Chains / 1,4-alpha-Glucan Branching Enzyme Type of study: Evaluation_studies Limits: Animals Language: En Journal: Nat Biotechnol Journal subject: BIOTECNOLOGIA Year: 2003 Document type: Article Affiliation country:
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