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Antimicrobial Agents and Chemotherapy, September 2007, p. 3322-3328, Vol. 51, No. 9
0066-4804/07/$08.00+0 doi:10.1128/AAC.00366-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

John R. Schreiber,2,
and
J. Christopher Hall1*
Department of Environmental Biology, University of Guelph, Guelph, Ontario, N1G 2W1 Canada,1 Department of Pediatrics, Case Western Reserve University, Cleveland Ohio 441062
Received 19 March 2007/ Returned for modification 18 April 2007/ Accepted 14 June 2007
The production of a recombinant human IgG1 in transgenic tobacco was examined to determine whether a plant-derived antibody could recruit immune system effector function against a bacterial pathogen. A plant transformation vector was engineered to contain genes for a human kappa light chain and a human gamma-1 heavy chain with VH and VL sequences from a previously identified human IgG2 monoclonal antibody (MAb) that specifically binds to and opsonizes Pseudomonas aeruginosa serotype O6ad. Unique NcoI and NotI restriction sites were incorporated to flank these variable sequences, resulting in a plant transformation vector that could be engineered for expression of any other human IgG1 antibody, requiring only the substitution of other VH and VL antigen-binding coding sequences. The plant-produced IgG1 was determined to have high-mannose glycan content and to be capable of mediating opsonophagocytosis of P. aeruginosa serotype O6ad in vitro using human complement and human polymorphonuclear leukocytes. Thus, MAbs produced in plants from this vector could provide human IgG1 MAbs for targeting other pathogens that require the recruitment of immune system effector functions.
Published ahead of print on 2 July 2007.
Present address: Tufts-Floating Hospital for Children, 750 Washington St., Boston, MA 02111.
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