1. Secretion of biologically active murine interleukin-2 by Lactococcus lactis subsp. lactis
- Author
-
Joël Vandekerckhove, Jm Wells, Alex Raeymaekers, Erik Remaut, Walter Fiers, and Lothar Steidler
- Subjects
Sequence analysis ,Molecular Sequence Data ,DNA, Recombinant ,Biology ,Applied Microbiology and Biotechnology ,law.invention ,Bacteriophage ,Mice ,law ,Gene expression ,Animals ,Life Science ,Secretion ,Amino Acid Sequence ,Gene ,Peptide sequence ,Base Sequence ,Ecology ,Lactococcus lactis ,biology.organism_classification ,Molecular biology ,Recombinant Proteins ,Genes, Bacterial ,Recombinant DNA ,Interleukin-2 ,Protein Processing, Post-Translational ,Research Article ,Plasmids ,Food Science ,Biotechnology - 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.
- Published
- 1995