Efficient production of N-terminally truncated biologically active human interleukin-6 by Bacillus brevis

• Published in: Bioscience, biotechnology, and biochemistry Vol. 64; no. 3; pp. 665 - 669
• Main Authors: Shiga, Y. (Tokyo Univ. of Pharmacy and Life Science, Hachioji (Japan)), Maki, M, Ohta, T, Tokishita, S, Okamoto, A, Tsukagoshi, N, Udaka, S, Konishi, A, Kodama, Y, Ejima, D, Matsui, H, Yamagata, H
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.03.2000; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Amino Acid Sequence; Antineoplastic drugs. Cytokines; BACILLUS; Bacillus - genetics; Bacillus brevis; Base Sequence; Biological and medical sciences; BIOLOGICAL PROPERTIES; Biotechnology; DNA, Complementary; Fundamental and applied biological sciences. Psychology; GENERO HUMANO; GENRE HUMAIN; Health. Pharmaceutical industry; human interleukin-6; Humans; Industrial applications and implications. Economical aspects; Interleukin-6 - biosynthesis; Interleukin-6 - genetics; INTERLEUKINE; INTERLEUKINS; INTERLEUQUINAS; MANKIND; Molecular Sequence Data; N-terminal truncation; Production of active biomolecules; PROPIEDADES BIOLOGICAS; PROPRIETE BIOLOGIQUE; Recombinant Proteins - biosynthesis; Recombinant Proteins - genetics; secretion; signal peptide; Human; Interleukin 6; Leader peptide; Brevibacillus brevis; Secretion; Cytokine; Bacteria; Recombinant protein; Gene expression; N terminal peptide; Fusion protein; Vector
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.64.665

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