Production and secretion of recombinant proteins in dictyostelium discoideum

Werner Dittrich; Keith L. Williams; Martin B. Slade

doi:10.1038/nbt0694-614

Production and secretion of recombinant proteins in dictyostelium discoideum

Werner Dittrich, Keith L. Williams^*, Martin B. Slade

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

34 Citations (Scopus)

Abstract

We have expressed useful amounts of three recombinant proteins in a new eukaryotic host/vector system. The cellular slime mold Dictyostelium discoideum efficiently secreted two recombinant products, a soluble form of the normally cell surface associated D. discoideum glycoprotein (PsA) and the heterologous protein glutathione-S-transferase (GST) from Schistosoma japonicum, while the enzyme β-glucuronidase (GUS) from Escherichia coli was cell associated. Up to 20mg/l of recombinant PsA and 1mg/l of GST were obtained after purification from a standard, peptone based growth medium. The secretion signal peptide was correctly cleaved from the recombinant GST- and PsA-proteins and the expression of recombinant PsA was shown to be stable for at least one hundred generations in the absence of selection.

Original language	English
Pages (from-to)	614-618
Number of pages	5
Journal	Bio/Technology
Volume	12
Issue number	6
DOIs	https://doi.org/10.1038/nbt0694-614
Publication status	Published - 1994

Access to Document

10.1038/nbt0694-614

Cite this

@article{ca4acceb8dae455198713a1db068a84e,

title = "Production and secretion of recombinant proteins in dictyostelium discoideum",

abstract = "We have expressed useful amounts of three recombinant proteins in a new eukaryotic host/vector system. The cellular slime mold Dictyostelium discoideum efficiently secreted two recombinant products, a soluble form of the normally cell surface associated D. discoideum glycoprotein (PsA) and the heterologous protein glutathione-S-transferase (GST) from Schistosoma japonicum, while the enzyme β-glucuronidase (GUS) from Escherichia coli was cell associated. Up to 20mg/l of recombinant PsA and 1mg/l of GST were obtained after purification from a standard, peptone based growth medium. The secretion signal peptide was correctly cleaved from the recombinant GST- and PsA-proteins and the expression of recombinant PsA was shown to be stable for at least one hundred generations in the absence of selection.",

author = "Werner Dittrich and Williams, {Keith L.} and Slade, {Martin B.}",

year = "1994",

doi = "10.1038/nbt0694-614",

language = "English",

volume = "12",

pages = "614--618",

journal = "Bio/Technology",

issn = "0733-222X",

publisher = "Springer, Springer Nature",

number = "6",

}

TY - JOUR

T1 - Production and secretion of recombinant proteins in dictyostelium discoideum

AU - Dittrich, Werner

AU - Williams, Keith L.

AU - Slade, Martin B.

PY - 1994

Y1 - 1994

N2 - We have expressed useful amounts of three recombinant proteins in a new eukaryotic host/vector system. The cellular slime mold Dictyostelium discoideum efficiently secreted two recombinant products, a soluble form of the normally cell surface associated D. discoideum glycoprotein (PsA) and the heterologous protein glutathione-S-transferase (GST) from Schistosoma japonicum, while the enzyme β-glucuronidase (GUS) from Escherichia coli was cell associated. Up to 20mg/l of recombinant PsA and 1mg/l of GST were obtained after purification from a standard, peptone based growth medium. The secretion signal peptide was correctly cleaved from the recombinant GST- and PsA-proteins and the expression of recombinant PsA was shown to be stable for at least one hundred generations in the absence of selection.

AB - We have expressed useful amounts of three recombinant proteins in a new eukaryotic host/vector system. The cellular slime mold Dictyostelium discoideum efficiently secreted two recombinant products, a soluble form of the normally cell surface associated D. discoideum glycoprotein (PsA) and the heterologous protein glutathione-S-transferase (GST) from Schistosoma japonicum, while the enzyme β-glucuronidase (GUS) from Escherichia coli was cell associated. Up to 20mg/l of recombinant PsA and 1mg/l of GST were obtained after purification from a standard, peptone based growth medium. The secretion signal peptide was correctly cleaved from the recombinant GST- and PsA-proteins and the expression of recombinant PsA was shown to be stable for at least one hundred generations in the absence of selection.

UR - http://www.scopus.com/inward/record.url?scp=0028242312&partnerID=8YFLogxK

U2 - 10.1038/nbt0694-614

DO - 10.1038/nbt0694-614

M3 - Article

C2 - 7764951

AN - SCOPUS:0028242312

SN - 0733-222X

VL - 12

SP - 614

EP - 618

JO - Bio/Technology

JF - Bio/Technology

IS - 6

ER -

Production and secretion of recombinant proteins in dictyostelium discoideum

Abstract

Access to Document

Other files and links

Fingerprint

Cite this