http://www.cnr.it/ontology/cnr/individuo/prodotto/ID231202
Assembly, Secretion and Vacuolar Delivery of a Hybrid Immunoglobulin in Plants (Articolo in rivista)
- Type
- Label
- Assembly, Secretion and Vacuolar Delivery of a Hybrid Immunoglobulin in Plants (Articolo in rivista) (literal)
- Anno
- 2000-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1104/pp.123.4.1483 (literal)
- Alternative label
L. Frigerio, ND. Vine, E. Pedrazzini, MB. Hein, F. Wang, JK.-C. Ma and A. Vitale (2000)
Assembly, Secretion and Vacuolar Delivery of a Hybrid Immunoglobulin in Plants
in Plant physiology (Online)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- L. Frigerio, ND. Vine, E. Pedrazzini, MB. Hein, F. Wang, JK.-C. Ma and A. Vitale (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.plantphysiol.org/content/123/4/1483.full (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- LF: Department of Biological Sciences, University of Warwick, Coventry, UK;
JKCM, NDV: Department of Oral Medicine and Pathology, Unit of Immunology, Guy's, King's and St. Thomas' Institute of Medicine and Dentistry, Guy's Hospital, London UK;
EP: Centro di Farmacologia Cellulare e Molecolare, Consiglio Nazionale delle Ricerche, Milano, Italy;
MBH, FW: The Scripps Research Institute, La Jolla, CA, USA;
AV: Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, Milano, Italy; (literal)
- Titolo
- Assembly, Secretion and Vacuolar Delivery of a Hybrid Immunoglobulin in Plants (literal)
- Abstract
- 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. (literal)
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