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Assembly, secretion, and vacuolar delivery of a hybrid immunoglobulin in plants
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UNSPECIFIED (2000) Assembly, secretion, and vacuolar delivery of a hybrid immunoglobulin in plants. PLANT PHYSIOLOGY, 123 (4). pp. 1483-1493. ISSN 0032-0889.
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Abstract
Secretory immunoglobulin (Ig) A is a decameric Ig composed of four a-heavy chains, four light chains, a joining CT) chain, and a secretory component (SC). The heavy and light chains form two tetrameric Ig molecules that are joined by the I 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 gamma-chain domains linked to constant region domains of an IgA alpha-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 I chain are responsible for vacuolar delivery, because IgA/G tetramers have the same fate. The parent IgG tetrameric molecule, containing wild-type gamma-heavy chains, is instead secreted rapidly and efficiently. This strongly suggests that intracellular retention and vacuolar delivery of IgA/G is due to the rr-domains present in the hybrid alpha/gamma-heavy chains and indicates that the plant secretory system may partially deliver to the vacuole recombinant proteins expected to be secreted.
Item Type: | Journal Article | ||||
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Subjects: | S Agriculture > SB Plant culture | ||||
Journal or Publication Title: | PLANT PHYSIOLOGY | ||||
Publisher: | AMER SOC PLANT PHYSIOLOGISTS | ||||
ISSN: | 0032-0889 | ||||
Official Date: | August 2000 | ||||
Dates: |
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Volume: | 123 | ||||
Number: | 4 | ||||
Number of Pages: | 11 | ||||
Page Range: | pp. 1483-1493 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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