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

doi:10.1128/aem.61.4.1627-1629.1995

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 journal › Article › Academic › peer-review

69 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 language	English
Pages (from-to)	1627-1629
Number of pages	3
Journal	Applied and Environmental Microbiology
Volume	61
Issue number	4
DOIs	https://doi.org/10.1128/aem.61.4.1627-1629.1995
Publication status	Published - Apr 1995
Externally published	Yes

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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.",

author = "L. Steidler and J.M. Wells and A. Raeymaekers and J. Vandekerckhove and W. Fiers and E. Remaut",

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AU - Steidler, L.

AU - Wells, J.M.

AU - Raeymaekers, A.

AU - Vandekerckhove, J.

AU - Fiers, W.

AU - Remaut, E.

PY - 1995/4

Y1 - 1995/4

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AB - 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.

U2 - 10.1128/aem.61.4.1627-1629.1995

DO - 10.1128/aem.61.4.1627-1629.1995

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SN - 0099-2240

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EP - 1629

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

IS - 4

ER -

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

Abstract

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