Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1991-05-21
1998-02-10
Rories, Charles C. P.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
435 701, 4351723, 4352404, 4353201, 800205, 800250, 800255, 800DIG42, 800DIG43, 800DIG56, 536 234, 536 235, 47 58, 530363, C12N 1582, C12N 1514, A01H 500, A01H 100
Patent
active
057168024
DESCRIPTION:
BRIEF SUMMARY
FIELD OF THE INVENTION
The present invention is in the field of recombinant DNA technology, more in particular recombinant DNA technology concerning the genetic manipulation of plants and is related to a process for the production of proteins or polypeptides using genetically manipulated plants or plant cells, as well as to the genetically manipulated plants and plant cells per se (including parts of the genetically manipulated plants), the heterologous protein material (e.g. a protein, polypeptide and the like) which is produced with the aid of these genetically manipulated plants or plant cells, and the recombinant polynucleotides (DNA or RNA) that are used for the genetic manipulation.
STATE OF THE ART
One of the results of biotechnology is the development of new production methods for proteins. In virtue of this, it is possible to accomplish that, on a preparative scale, microorganisms containing recombinant DNA produce proteins which these microorganisms naturally do not synthesize, or naturally do not synthesize in those quantitities. Recent examples are in particular insulin, various interferon types and human growth hormone that are produced in commercial quantities by, among others, bacteria and yeast cells.
Characteristic for these examples is the fact that this often concerns relatively simple polypeptides that do not require co- or post-translational processing within the cell, to obtain their final form and biological function. For a large number of more complex proteins of higher organisms, such a processing is of concern for the functioning of those proteins. For example, they need to be correctly glycosylated or undergo a membrane passage during which signal peptides are split off from a precursor (`precursor-protein`). In prokaryotic microorganisms this is not possible, due to which higher organisms such as fungi have to be used.
Proteins synthesized on the rough endoplasmatic reticulum (ER) are excreted by the eukaryotic cell or stored at specific locations in the excretion route like the ER, Golgi complex, plasma membrane or vacuole/lysosome (Pfeffer & Rothman, 1987). The choice of the excretion route is determined by the presence of a hydrophobic, amino-terminal signal peptide that is cleaved off from the precursor-protein. Examples of this are signal peptides for invertase (Carlston & Botstein, 1982) or .alpha.-factor (Herskowitz & Oshima, 1982) that cause the respective mature protein products to reach the periplasmic space. Recently it was shown that signal peptides can also be used to achieve excretion of human proteins by yeast cells, although in that case processing is not complete (Stetler et al., 1989).
From the experiments with the synthesis of animal proteins in fungi, it appeared that the use of fungal signal peptides gives more efficient processing and excretion than animal signal peptides, which means that a signal peptide, derived from the fungus which is acting as host, is functioning better (Kingsman et al., 1987; Harkki et al., 1989).
For the transport to the lysosomes in mammals (Kornfeld., 1987), or vacuoles in yeast (Johnsson et al., 1987) and plant cells (Dorel et al., 1989) additional information is required that is located in part of the sequence of the mature protein itself.
The knowledge of signal peptides for the excretion by plant cells is still very limited (Della-Cioppa et al., 1987). Such signal peptides have only been described for 2 extensins from carrot (Chen & Varner, 1985) and tobacco (memelink, 1988), as well as for three pathogenesis-related (PR) proteins from tobacco (Hooft van Huijsduijnen et al., 1985; Cornelissen et al., 1986); De Loose et al., 1988). From this small number of signal peptides no consensus has been obtained on the characteristics of cleavage- or recognition-sites. Neither has it become clear whether proteins, that are foreign to the plant, can be excreted by plant cells, nor if the processing of the signal peptide occurs correctly when a fusion construct between a plant signal peptide and a heterologous protein would be used.
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Dekker Bernardus Martinus M.
Hoekema Andreas
Schrammeijer Barbara
Sijmons Peter Christiaan
Van Den Elzen Peturs Josephus M.
Mogen International N.V.
Rories Charles C. P.
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