UNSPECIFIED. (2002) ER-resident chaperone interactions with recombinant antibodies in transgenic plants. EUROPEAN JOURNAL OF BIOCHEMISTRY, 269 (24). pp. 6042-6051. ISSN 0014-2956

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Abstract

In this study, we demonstrate that the folding and assembly of IgG in transgenic tobacco plants is orchestrated by BiP (binding protein), an endoplasmic reticulum resident chaperone. Expression of BiP and calreticulin was examined in transgenic tobacco plants that express immunoglobulin chains, either singly or in combination to form IgG antibody. BiP mRNA expression was lowest in wild-type nontransformed plants and those that expressed immunoglobulin light chain alone. Higher mRNA levels were detected in plants expressing fully assembled immunoglobulin (light and heavy chains), and the most abundant levels of RNA transcript were found in those plants that expressed immunoglobulin heavy chain alone. Estimation of total BiP demonstrated a similar pattern, with the highest levels detected in plants expressing immunoglobulin heavy chain alone. Immunoprecipitation studies demonstrated that BiP was associated with immunoglobulin chains extracted from protoplast lysates, but not from secreted fluids. Again, most BiP was coprecipitated from plants expressing heavy chain only and those that produced full length IgG. The binding of BiP to Ig heavy chains was ATP-sensitive. Co-expression of heavy and light chain resulted in IgG assembly and displacement of BiP from the heavy chain as the amount of light chain increased. Although calreticulin mRNA and total protein levels varied in a similar manner to those of BiP in the transgenic plants, there was no evidence for association between calreticulin and Ig chains, by coimmunoprecipitation. The results indicate that BiP, but not calreticulin, takes part in immunoglobulin folding and assembly in transgenic plants.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	EUROPEAN JOURNAL OF BIOCHEMISTRY
Publisher:	BLACKWELL PUBLISHING LTD
ISSN:	0014-2956
Date:	December 2002
Volume:	269
Number:	24
Number of Pages:	10
Page Range:	pp. 6042-6051
Identification Number:	10.1046/j.1432-1033.2002.03302.x
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/10233

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