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A functional antibody lacking N-linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll protoplasts
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UNSPECIFIED (2005) A functional antibody lacking N-linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll protoplasts. PLANT BIOTECHNOLOGY JOURNAL, 3 (5). pp. 497-504. doi:10.1111/j.1467-7652.2005.00140.x ISSN 1467-7644.
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Official URL: http://dx.doi.org/10.1111/j.1467-7652.2005.00140.x
Abstract
A potential drawback in the use of plants as an expression platform for pharmaceutical proteins such as antibodies is that plant-specific N-glycosylation can result in proteins with altered function and potential antigenicity. In many cases, the N-glycans are essential for the correct folding, assembly and transport of the recombinant proteins. We tested whether progressive removal of glycosylation sites had a detrimental effect on the synthesis, assembly and secretion of a plant-made immunoglobulin G, Guy's 13. Our results indicate that the plant secretory pathway can cope well with aglycosylated antibody chains. The immunoglobulin without N-linked glycans is correctly assembled and secreted by tobacco protoplasts. Capture enzyme-linked immunosorbent assay also shows that antigen-binding properties are unaffected. Our results therefore suggest one possible alternative to the engineering of a humanized glycosylation machinery in plants.
Item Type: | Journal Article | ||||
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Subjects: | T Technology > TP Chemical technology S Agriculture > SB Plant culture |
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Journal or Publication Title: | PLANT BIOTECHNOLOGY JOURNAL | ||||
Publisher: | BLACKWELL PUBLISHING | ||||
ISSN: | 1467-7644 | ||||
Official Date: | September 2005 | ||||
Dates: |
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Volume: | 3 | ||||
Number: | 5 | ||||
Number of Pages: | 8 | ||||
Page Range: | pp. 497-504 | ||||
DOI: | 10.1111/j.1467-7652.2005.00140.x | ||||
Publication Status: | Published |
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