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Plant and Cell Physiology, 1998, Vol. 39, No. 6 639-646
© 1998

Article

Accumulation Pattern of IgG Antibodies and Fab Fragments in Transgenic Arabidopsis thaliana Plants

Chris De Wilde1, Riet De Rycke1, Tom Beeckman2, Myriam De Neve1, Marc Van Montagu1, Gilbert Engler3 and Ann Depicker1,4

1 Laboratorium voor Genetics, Department of Genetics, Flanders Interuniversity Institute for Biotechnology, Universiteit Gent B-9000 Gent, Belgium
2 Laboratorium voor Morfologie, Systematiek en Ecologie van de Planten, Universiteit Gent B-9000 Gent, Belgium
3 Laboratoire Associé de I'lnstitut National de la Recherche Agronomique (France), Universiteit Gent B-9000 Gent, Belgium

For the further optimization of antibody expression in plants, it is essential to determine the final accumulation sites of plant-made antibodies. Previously, we have shown that, upon secretion, IgG antibodies and Fab fragments can be detected in the intercellular spaces of leaf mesophyil cells of transgenic Arabidopsis thaliana plants. However, immunofluorescence microscopy showed that this is probably not their final accumulation site. In leaves, IgG and Fabfragments accumulate also at the interior side of the epidermal cell layers and in xylem vessels. These accumulation sites correspond with the leaf regions where water of the transpiration stream is entering a space impermeable to the proteins or where water is evaporating. In roots, plant-made Fab fragments accumulate in intercellular spaces of cortex cells, in the cytoplasm of pericycle and, to a lesser extent, endodermis cells, and in cells of the vascular cylinder. In other words, antibody accumulation occurs at the sites where water passes on its radial pathway towards and within the vascular bundle. Taken together, our results suggest that, upon secretion of plant-made antibodies or Fab fragments, a large proportion of these proteins are transported in the apoplast of A. thaliana, possibly by the water flow in the transpiration stream.

4Corresponding author. Fax 32-9-2645349; e-mail: anpic{at}gengenp.rug.ac.be

(Received December 27, 1997; Accepted April 6, 1998)
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