TY - JOUR
T1 - Production of small antibacterial peptides using silkworm-baculovirus protein expression system
AU - Fukushima, Mai
AU - Iiyama, Kazuhiro
AU - Yamashita, Jun
AU - Furue, Masutaka
AU - Tsuji, Gaku
AU - Imanishi, Shigeo
AU - Mon, Hiroaki
AU - Lee, Jae Man
AU - Kusakabe, Takahiro
N1 - Funding Information:
This work was supported in part by grants, KAKENHI numbers 22248003 and 22248004, from the Japan Society for the Promotion of Science.
PY - 2013/8/18
Y1 - 2013/8/18
N2 - The recombinant proteins with strong antimicrobial activity are known to be very difficult to express using bacterial expression system. Here, human β-defensin (DEFB) 1, DEFB2, and DEFB3 were successfully produced using a silkworm-baculovirus protein expression system. We have generated four baculoviruses for each DEFB protein to compare the effect of different peptide tags in secretion into silkworm larval hemolymph. Interestingly, the best performing peptide tags for the secretion were different among DEFBs: C-terminal GST-H8 tag for DEFB1, N-terminal H8 tag for DEFB2, and C-terminal H8 tag for DEFB3, respectively. In addition, the colony count assay demonstrated that the recombinant DEFB2 s showed antimicrobial activities against Escherichia coli, Pseudomonas aeruginosa, and Paenibacillus thiaminolyticus.
AB - The recombinant proteins with strong antimicrobial activity are known to be very difficult to express using bacterial expression system. Here, human β-defensin (DEFB) 1, DEFB2, and DEFB3 were successfully produced using a silkworm-baculovirus protein expression system. We have generated four baculoviruses for each DEFB protein to compare the effect of different peptide tags in secretion into silkworm larval hemolymph. Interestingly, the best performing peptide tags for the secretion were different among DEFBs: C-terminal GST-H8 tag for DEFB1, N-terminal H8 tag for DEFB2, and C-terminal H8 tag for DEFB3, respectively. In addition, the colony count assay demonstrated that the recombinant DEFB2 s showed antimicrobial activities against Escherichia coli, Pseudomonas aeruginosa, and Paenibacillus thiaminolyticus.
UR - http://www.scopus.com/inward/record.url?scp=84879101133&partnerID=8YFLogxK
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U2 - 10.1080/10826068.2012.762717
DO - 10.1080/10826068.2012.762717
M3 - Article
C2 - 23742088
AN - SCOPUS:84879101133
SN - 1082-6068
VL - 43
SP - 565
EP - 576
JO - Preparative Biochemistry and Biotechnology
JF - Preparative Biochemistry and Biotechnology
IS - 6
ER -