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Plant Physiol, August 2000, Vol. 123, pp. 1483-1494
Assembly, Secretion, and Vacuolar Delivery of a Hybrid
Immunoglobulin in Plants
Lorenzo
Frigerio,
Nicholas D.
Vine,
Emanuela
Pedrazzini,
Mich B.
Hein,
Fei
Wang,
Julian K.-C.
Ma,1 and
Alessandro
Vitale1*
Department of Biological Sciences, University of Warwick, Coventry
CV4 7AL, United Kingdom (L.F.); Department of Oral Medicine and
Pathology, Unit of Immunology, Guy's, King's and St. Thomas'
Institute of Medicine and Dentistry, Guy's Hospital, Guy's Tower, St.
Thomas's Street, London SE1 9RT, United Kingdom (N.D.V., J.K.-C.M.);
Centro di Farmacologia Cellulare e Molecolare, Consiglio Nazionale
delle Ricerche, via Vanvitelli 32, 20129 Milano, Italy (E.P.);
The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla,
California 92037 (M.B.H., F.W.); and Istituto Biosintesi Vegetali,
Consiglio Nazionale delle Ricerche, via Bassini 15, 20133 Milano, Italy
(A.V.)
Secretory immunoglobulin (Ig) A is a decameric Ig composed
of four  -heavy chains, four light chains, a joining (J) chain, and a
secretory component (SC). The heavy and light chains form two
tetrameric Ig molecules that are joined by the J chain and associate
with the SC. Expression of a secretory monoclonal antibody in tobacco
(Nicotiana tabacum) has been described: this molecule (secretory IgA/G [SIgA/G]) was modified by having a hybrid heavy chain sequence consisting of IgG  -chain domains linked to constant region domains of an IgA -chain. In tobacco, about 70% of the protein assembles to its final, decameric structure. We show here that
SIgA/G assembly and secretion are slow, with only approximately 10% of
the newly synthesized molecules being secreted after 24 h and the
bulk probably remaining in the endoplasmic reticulum. In addition, a
proportion of SIgA/G is delivered to the vacuole as at least partially
assembled molecules by a process that is blocked by the membrane
traffic inhibitor brefeldin A. Neither the SC nor the J chain are
responsible for vacuolar delivery, because IgA/G tetramers have the
same fate. The parent IgG tetrameric molecule, containing wild-type
-heavy chains, is instead secreted rapidly and efficiently. This
strongly suggests that intracellular retention and vacuolar delivery of
IgA/G is due to the -domains present in the hybrid /-heavy
chains and indicates that the plant secretory system may partially
deliver to the vacuole recombinant proteins expected to be
secreted.
1
These authors contributed equally to the paper.
*
Corresponding author; e-mail vitale{at}icm.mi.cnr.it; fax
39-02-23699411.
© 2000 American Society of Plant Physiologists
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