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The c-terminal extension of a hybrid immunoglobulin A/G heavy chain is responsible for its Golgi-mediated sorting to the vacuole

By Jane L. Hadlington, Aniello Santoro, James Nuttall, J. (Jurgen) Denecke, Julian K.-C. Ma, A. (Alessandro) Vitale and Lorenzo Frigerio

Abstract

We have assessed the ability of the plant secretory pathway to handle the expression of complex heterologous proteins by investigating the fate of a hybrid immunoglobulin A/G in tobacco cells. Although plant cells can express large amounts of the antibody, a relevant proportion is normally lost to vacuolar sorting and degradation. Here we show that the synthesis of high amounts of IgA/G does not impose stress on the plant secretory pathway. Plant cells can assemble antibody chains with high efficiency and vacuolar transport occurs only after the assembled immunoglobulins have traveled through the Golgi complex. We prove that vacuolar delivery of IgA/G depends on the presence of a cryptic sorting signal in the tailpiece of the IgA/G heavy chain. We also show that unassembled light chains are efficiently secreted as monomers by the plant secretory pathway

Topics: QK, QR
Publisher: American Society for Cell Biology
Year: 2003
OAI identifier: oai:wrap.warwick.ac.uk:941

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  1. (1996). A pathway for targeting soluble misfolded proteins to the yeast vacuole. doi
  2. (1994). A simpler sort of antibody. doi
  3. (2001). A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. doi
  4. (2003). Assembly of immunoglobulin light chains as a prerequisite for secretion. doi
  5. (1994). Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants. doi
  6. (2000). Assembly, secretion and vacuolar delivery of a hybrid immunoglobulin in plants. doi
  7. (1997). Coexpression of the maize -zein and -zein genes results in stable accumulation of -zein in endoplasmic reticulum-derived protein bodies fromed by -zein. doi
  8. (1993). Determination of the functional elements within the vacuolar targeting signal of barley lectin. doi
  9. (1998). Engineering plant protein composition for improved nutrition. doi
  10. (2002). ER-resident chaperone interactions with recombinant antibodies in transgenic plants. doi
  11. (1991). Expression of wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport. doi
  12. (1998). Free ricin A chain, proricin and native toxin have different cellular fates when expressed in tobacco protoplasts. doi
  13. (1995). Generation and assembly of secretory antibodies in plants. doi
  14. (1987). Immunoglobulin A (IgA): molecular and cellular interactions involved in IgA biosynthesis and immune response. doi
  15. (2001). Influence of KDEL on the fate of trimeric or assembly-defective phaseolin: selective use of an alternative route to vacuoles. doi
  16. (2000). Mass transport of proform of a KDEL-tailed cysteine protease (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds. doi
  17. (2001). Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. doi
  18. (1994). Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space. doi
  19. (1992). Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope.
  20. (1999). Production of recombinant proteins in plant root exudates. doi
  21. (2001). Production of secretory IgA antibodies in plants. doi
  22. (1997). Protein quality control along the route to the plant vacuole. doi
  23. (1990). Protein secretion in plant cells can occur via a default pathway. doi
  24. (1999). Saturation of the endoplasmic reticulum retention machinery reveals anterograde bulk flow. doi
  25. (2001). Secretory bulk flow of soluble proteins is efficient and COPII dependent. doi
  26. (1998). Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide. doi
  27. (1999). The endoplasmic reticulum— gateway of the secretory pathway. doi
  28. (2001). The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation. doi
  29. (1998). The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. doi
  30. (1996). The maize -zein sequesters -zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. doi
  31. (1999). The N-terminal propeptide and the C-terminus of the precursor to 20-kilo-dalton potato tuber protein can function as different types of vacuolar sorting signals. doi
  32. (1998). Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles. doi
  33. (1999). What do proteins need to reach different vacuoles? doi

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