A functional antibody lacking N-linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll protoplasts
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. ISSN 1467-7644Full text not available from this repository.
Official URL: http://dx.doi.org/10.1111/j.1467-7652.2005.00140.x
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|
|Subjects:||T Technology > TP Chemical technology
S Agriculture > SB Plant culture
|Journal or Publication Title:||PLANT BIOTECHNOLOGY JOURNAL|
|Official Date:||September 2005|
|Number of Pages:||8|
|Page Range:||pp. 497-504|
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