Production in Escherichia coli of Moricin, a Novel Type Antibacterial Peptide from the Silkworm,Bombyx mori

1996 ◽  
Vol 220 (3) ◽  
pp. 664-669 ◽  
Author(s):  
Seiichi Hara ◽  
Minoru Yamakawa
Keyword(s):  
Escherichia Coli ◽  
Bombyx Mori ◽  
Antibacterial Peptide ◽  
Silkworm Bombyx Mori

A novel Rel protein and shortened isoform that differentially regulate antibacterial peptide genes in the silkworm Bombyx mori

2005 ◽  
Vol 1730 (1) ◽  
pp. 10-21 ◽  
Author(s):  
Hiromitsu Tanaka ◽  
Masafumi Yamamoto ◽  
Yuko Moriyama ◽  
Masafumi Yamao ◽  
Seiichi Furukawa ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Antibacterial Peptide ◽  
Silkworm Bombyx Mori

scholarly journals Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori

FEBS Letters ◽  
2002 ◽  
Vol 518 (1-3) ◽  
pp. 33-38 ◽  
Author(s):  
Hikaru Hemmi ◽  
Jun Ishibashi ◽  
Seiichi Hara ◽  
Minoru Yamakawa
Keyword(s):  
Bombyx Mori ◽  
Solution Structure ◽  
Antibacterial Peptide ◽  
Silkworm Bombyx Mori

scholarly journals Eclosion hormone of the silkworm Bombyx mori Expression in Escherichia coli and location of disulfide bonds

FEBS Letters ◽  
1990 ◽  
Vol 263 (2) ◽  
pp. 358-360 ◽  
Author(s):  
Takaharu Kono ◽  
Hiromichi Nagasawa ◽  
Hiroshi Kataoka ◽  
Akira Isogai ◽  
Hajime Fugo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bombyx Mori ◽  
Disulfide Bonds ◽  
Eclosion Hormone ◽  
Expression In Escherichia Coli ◽  
Silkworm Bombyx Mori

scholarly journals A novel antibacterial peptide family isolated from the silkworm, Bombyx mori

1995 ◽  
Vol 310 (2) ◽  
pp. 651-656 ◽  
Author(s):  
S Hara ◽  
M Yamakawa
Keyword(s):  
Bombyx Mori ◽  
Antibacterial Peptide ◽  
Bacterial Membrane ◽  
Antibacterial Peptides ◽  
The Novel ◽  
Threonine Residue ◽  
Peptide Family ◽  
Liposome Preparation ◽  
Low Ionic Strength ◽  
Silkworm Bombyx Mori

Three structurally related and novel antibacterial peptides have been isolated from the haemolymph of the silkworm, Bombyx mori, immunized with Escherichia coli. These peptides were 32 amino acids long and characteristically rich in proline residues. A unique threonine residue in each peptide was O-glycosylated and the modification seemed to be important for expression of antibacterial activity. The primary structure and antibacterial character of the novel peptides resemble those of abaecin (41% identity in amino acid sequence), an antibacterial peptide of the honeybee, although abaecin is not O-glycosylated. Incubation of the novel peptides with a liposome preparation caused leakage of entrapped glucose under low-ionic-strength conditions, suggesting that a target of the peptides is the bacterial membrane. We propose the name ‘lebocin’ for the novel peptide family isolated from B. mori.

scholarly journals Inducible gene expression of moricin, a unique antibacterial peptide from the silkworm (Bombyx mori)

1999 ◽  
Vol 340 (1) ◽  
pp. 265-271 ◽  
Author(s):  
Seiichi FURUKAWA ◽  
Hiromitsu TANAKA ◽  
Hiroshi NAKAZAWA ◽  
Jun ISHIBASHI ◽  
Toshio SHONO ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Binding Site ◽  
Bombyx Mori ◽  
Regulatory Region ◽  
Antibacterial Peptide ◽  
Nucleotide Sequencing ◽  
Nuclear Factor ◽  
E Coli ◽  
Silkworm Bombyx Mori

Molecular cloning of cDNAs encoding moricin, a novel antibacterial peptide from the silkworm (Bombyx mori), was performed using a fat-body cDNA library. A reverse-transcription PCR product encoding a partial nucleotide sequence of moricin was used as a probe. Nucleotide sequencing of four positive clones revealed two types of moricin cDNAs designated moricin 1 and 2. cDNAs for moricin 1 and 2 shared 97.2% identity in their nucleotide sequences. Although one amino acid residue (Phe6) of moricin 1 in the putative signal peptide was replaced with Lys6 in moricin 2, amino acid sequences of their mature portions were identical. Moricin gene expression in B. mori larvae injected with Escherichia coli was observed in fat-bodies, haemocytes and the Malpighian tubule, but not in other tissues like the midgut and silk glands. Accumulation of moricin gene transcripts induced by E. coli reached a maximum level 8 h after injection and persisted up to 48 h. It was confirmed that lipopolysaccharide (LPS) and lipid A, which are cell-wall components of E. coli, triggered moricin gene expression. Comparison of gene expression between moricin 1 and 2 by PCR using specific primers indicated that moricin 2 gene was more strongly expressed than moricin 1 gene. A genomic clone encoding moricin 2 was screened from a B. mori genomic library using a moricin cDNA as a probe. Regulatory motifs for gene expression such as nuclear-factor-κB-binding-site-like sequence (ĸB site) and nuclear-factor-interleukin-6-binding-site-like sequence (NF-IL-6 site) were found in the 5ʹ-upstream regulatory region. An electrophoretic-mobility-shift assay revealed that there are bacterial LPS-inducible nuclear proteins that can bind to the ĸB site and other sites in the regulatory region.

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