Open AccessA functional antibody lacking N ‐linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll protoplasts
Author(s) -
Nuttall James,
Ma Julian K.C.,
Frigerio Lorenzo
Publication year - 2005
Publication title -
plant biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.525
H-Index - 115
eISSN - 1467-7652
pISSN - 1467-7644
DOI - 10.1111/j.1467-7652.2005.00140.x
Subject(s) - biology , glycan , protoplast , antibody , microbiology and biotechnology , computational biology , biochemistry , glycoprotein , genetics
Summary 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.