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

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.

Bacteria‐Based Materials for Stem Cell Engineering

“…L. lactis is a gram‐positive lactic acid bacterium that has been used for centuries in food fermentation. Within the last 35 years, significant progress has been made in using this organism, amongst other bacterial species in genetic engineering for the therapeutic delivery of proteins . For example, interleukin 27 has been expressed to alleviate the symptoms of colitis in mice .…”

Engineering of the gut commensal bacterium Bacteroides ovatus to produce and secrete biologically active murine interleukin-2 in response to xylan

“…Lactococcus lactis has been engineered to secrete IL10, which when administered intragastrically to two murine models of IBD was as effective as more conventional steroid therapy, in both preventing and treating disease (Steidler et al 2000). This Lactococcus system has also been used to produce biologically active IL2 and IL6 (Steidler et al 1995(Steidler et al , 1998. The advantage of this unique form of therapeutic delivery is that it is a convenient and simple means of delivering biologically active proteins directly to their site of action, avoiding the inconvenience and systemic exposure associated with parenteral therapy.…”

Construction of fusion vectors of corynebacteria: expression of glutathione-S-transferase fusion protein in Corynebacterium acetoacidophilum ATCC 21476

“…Secretory nature and no detectable extracellular proteases have been an advantage of this organism. Generally, food grade organisms such as Lactococcus lactis [2,3] are useful for the production of commercially important proteins.…”