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Vol. 14, Issue 6, 2592-2602, June 2003

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The C-terminal Extension of a Hybrid Immunoglobulin A/G Heavy Chain Is Responsible for Its Golgi-mediated Sorting to the Vacuole

Jane L. Hadlington ^* , Aniello Santoro  , James Nuttall ^*, Jürgen Denecke , Julian K-C. Ma ^¶, Alessandro Vitale  ^||, and Lorenzo Frigerio ^* ||

^* Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom; Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, 20133 Milano, Italy; Centre for Plant Sciences, Leeds Institute for Plant Biotechnology and Agriculture, School of Biology, The University of Leeds, Leeds LS2 9JT, United Kingdom; and ^¶ Unit of Immunology, Department of Oral Medicine and Pathology, Guy's Hospital, London SE1 9RT, United Kingdom

Submitted November 27, 2002; Revised February 19, 2003; Accepted February 26, 2003
Monitoring Editor: Maarten J. Chrispeels

We have assessed the ability of the plant secretory pathway to handle the expression of complex heterologous proteins by investigating the fate of a hybrid immunoglobulin A/G in tobacco cells. Although plant cells can express large amounts of the antibody, a relevant proportion is normally lost to vacuolar sorting and degradation. Here we show that the synthesis of high amounts of IgA/G does not impose stress on the plant secretory pathway. Plant cells can assemble antibody chains with high efficiency and vacuolar transport occurs only after the assembled immunoglobulins have traveled through the Golgi complex. We prove that vacuolar delivery of IgA/G depends on the presence of a cryptic sorting signal in the tailpiece of the IgA/G heavy chain. We also show that unassembled light chains are efficiently secreted as monomers by the plant secretory pathway.

^|| Corresponding authors. E-mail addresses: vitale{at}ibba.cnr.it; l.frigerio{at}warwick.ac.uk.

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