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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-12-15
pubmed:abstractText
To investigate the role of subunit assembly in the intracellular deposition of multimeric recombinant proteins, we expressed a partially humanized secretory immunoglobulin in rice endosperm cells and determined the subcellular locations of the assembled protein and its individual components. Transgenic rice plants expressing either individual subunits or all the subunits of the antibody were generated by particle bombardment, and protein localization was determined by immunoelectron microscopy. Assembly of the antibody was confirmed by immunoassay and coimmunoprecipitation. Immunolocalization experiments showed no evidence for secretion of the antibody or any of its components to the apoplast. Rather, the nonassembled light chain, heavy chain and secretory component accumulated predominantly within endoplasmic reticulum-derived protein bodies, while the assembled antibody, with antigen-binding function, accumulated specifically in protein storage vacuoles. These results show that the destination of a complex recombinant protein within the plant cell is influenced by its state of assembly.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jan
pubmed:issn
1467-7652
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-27
pubmed:year
2005
pubmed:articleTitle
A recombinant multimeric immunoglobulin expressed in rice shows assembly-dependent subcellular localization in endosperm cells.
pubmed:affiliation
John Innes Centre, Colney Lane, Norwich NR4 7UH, Norfolk, UK.
pubmed:publicationType
Journal Article