Efficient expression, processing and secretion of a biologically active mammalian protein by Vibrio cholerae

Anuja Ghorpade, Lalit C. Garg

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The use of Vibrio cholerae as a secretory expression system for the expression of a mammalian protein, namely human growth hormone, under the control of the heat labile enterotoxin chain B signal sequence is reported. The protein is efficiently expressed and processed. The mature protein is exported to the periplasm after which it is secreted to the extracellular milieu. The expressed and secreted hGH actively binds to its receptor as established by its receptor binding activity. The biological activity of the protein is demonstrated in vitro in a Nb2 proliferation assay.

Original languageEnglish
Pages (from-to)167-170
Number of pages4
JournalFEBS Letters
Volume387
Issue number2-3
DOIs
StatePublished - 3 Jun 1996

Fingerprint

Vibrio cholerae
Processing
Proteins
Periplasm
Human Growth Hormone
Enterotoxins
Protein Sorting Signals
Bioactivity
Assays
Hot Temperature

Keywords

  • Human growth hormone
  • Nb2 cell bioassay
  • Secretory expression
  • Signal sequence

Cite this

Ghorpade, Anuja ; Garg, Lalit C. / Efficient expression, processing and secretion of a biologically active mammalian protein by Vibrio cholerae. In: FEBS Letters. 1996 ; Vol. 387, No. 2-3. pp. 167-170.
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Efficient expression, processing and secretion of a biologically active mammalian protein by Vibrio cholerae. / Ghorpade, Anuja; Garg, Lalit C.

In: FEBS Letters, Vol. 387, No. 2-3, 03.06.1996, p. 167-170.

Research output: Contribution to journalArticle

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