PMID: 9537390Apr 16, 1998Paper

A nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactis

Journal of Bacteriology
Y Le LoirP Langella

Abstract

Lactococcus lactis, a gram-positive organism widely used in the food industry, is a potential candidate for the secretion of biologically useful proteins. We examined the secretion efficiency and capacity of L. lactis by using the Staphylococcus aureus nuclease (Nuc) as a heterologous model protein. When expressed in L. lactis from an efficient lactococcal promoter and its native signal peptide, only approximately 60% of total Nuc was present in a secreted form at approximately 5 mg per liter. The remaining 40% was found in a cell-associated precursor form. The secretion efficiency was reduced further to approximately 30% by the deletion of 17 residues of the Nuc native propeptide (resulting in NucT). We identified a modification which improved secretion efficiency of both native Nuc and NucT. A 9-residue synthetic propeptide, LEISSTCDA, which adds two negative charges at the +2 and +8 positions, was fused immediately after the signal peptide cleavage site. In the case of Nuc, secretion efficiency was increased to approximately 80% by LEISSTCDA insertion without altering the signal peptide cleavage site, and the yield was increased two- to fourfold (up to approximately 20 mg per liter). The improvement of NucT secretion efficie...Continue Reading

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Citations

Aug 30, 2001·Applied and Environmental Microbiology·Y Le LoirP Langella
Feb 2, 2002·Applied and Environmental Microbiology·L G Bermúdez-HumaránYves Le Loir
Jun 1, 2002·Applied and Environmental Microbiology·A MiyoshiP Langella
Oct 13, 2004·FEMS Microbiology Letters·Anderson MiyoshiVasco Azevedo
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Mar 10, 2015·Applied Microbiology and Biotechnology·Agnieszka WyszyńskaElżbieta Katarzyna Jagusztyn-Krynicka
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