Secretion of biologically active porcine interleukin-2 by Lactococcus lactis.
In this study, secretion of two functional recombinant porcine interleukin-2 (rIL-2) proteins by Lactococcus lactis was studied. Two secretion cassettes were constructed in which the secretion was achieved by gene fusion between the lactococcal usp45 secretion signal, a synthetic propeptide and the sequence encoding the mature IL-2. In addition, one of the two secretion cassettes contained the H-domains of L. lactis PrtP. Both of the constructed recombinant IL-2 proteins were found to be secreted in the same quantities, approximately 0.5mg/l. According to a cell proliferative assay using CTLL-2 cell line the specific biological activities of both purified rIL-2 proteins were found to be of similar levels.
Avall-Jääskeläinen
Silja
S
Department of Basic Veterinary Sciences, Division of Microbiology and Epidemiology, FIN-00014 University of Helsinki, Finland.
Palva
Airi
A
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western / Q000662:veterinary; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D005798:Genes, Bacterial; D005822:Genetic Vectors; D007376:Interleukin-2 / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D013294:Lactococcus lactis / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D013552:Swine
D007376:Interleukin-2; D011994:Recombinant Proteins