SECRETION OF BIOLOGICALLY-ACTIVE MURINE INTERLEUKIN-2 BY LACTOCOCCUS-LACTIS SUBSP LACTIS

Secretion of functional recombinant murine interleukin-2 (mIL2) by Lac tococcus lactis was achieved by fusion of the sequence encoding mature mIL2 to the secretion signal leader of the lactococcal usp45 gene pla ced under transcriptional control of the phage T7 promoter-T7 RNA poly merase expression system. The recombinant mature mIL2 was one of only a few proteins which accumulated in the growth medium. Sequence analys is revealed correct processing at the first amino acid of the mature p rotein. A T-cell proliferation assay showed that the recombinant prote in has the same specific biological activity as mIL2 obtained from a n atural source.