Secretion of biologically active murine interleukin-2 by Lactococcus lactis subsp. lactis

L. Steidler, J.M. Wells, A. Raeymaekers, J. Vandekerckhove, W. Fiers, E. Remaut*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

60 Citations (Scopus)

Abstract

Secretion of functional recombinant murine interleukin-2 (mIL2) by Lactococcus lactis was achieved by fusion of the sequence encoding mature mIL2 to the secretion signal leader of the lactococcal usp45 gene placed under transcriptional control of the phage T7 promoter-T7 RNA polymerase expression system. The recombinant mature mIL2 was one of only a few proteins which accumulated in the growth medium. Sequence analysis revealed correct processing at the first amino acid of the mature protein. A T-cell proliferation assay showed that the recombinant protein has the same specific biological activity as mIL2 obtained from a natural source.

Original languageEnglish
Pages (from-to)1627-1629
Number of pages3
JournalApplied and Environmental Microbiology
Volume61
Issue number4
DOIs
Publication statusPublished - Apr 1995
Externally publishedYes

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