Efficient production of N-terminally truncated biologically active human interleukin-6 by Bacillus brevis.
cDNAs encoding human interleukin 6 (hIL-6) and its variants lacking the N-terminal Pro and Pro-Val-Pro-Pro, respectively, were expressed in Bacillus brevis by using the signal peptide fusion approach. The presence of Pro at the N-terminus of the mature protein hindered the action of the Bacillus brevis signal peptidase. hIL-6 lacking the N-terminal Pro-Val-Pro-Pro was most efficiently secreted in a biologically active form and accumulated in the culture medium to a level of 200 mg per liter, which is the highest level reported for the bacterial secretion of hIL-6.
Shiga
Y
Y
School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Japan.
Maki
M
M
Ohta
T
T
Tokishita
S
S
Okamoto
A
A
Tsukagoshi
N
N
Udaka
S
S
Konishi
A
A
Kodama
Y
Y
Ejima
D
D
Matsui
H
H
Yamagata
H
H
D000595:Amino Acid Sequence; D001407:Bacillus / Q000235:genetics*; D001483:Base Sequence; D018076:DNA, Complementary; D006801:Humans; D015850:Interleukin-6 / Q000096:biosynthesis* / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D018076:DNA, Complementary; D015850:Interleukin-6; D011994:Recombinant Proteins