Characterization of a Bombyx mori cDNA encoding a novel member of the attacin family of insect antibacterial proteins

Sugiyama, Masao; Kuniyoshi, Hisato; Kotani, Eiji; Taniai, Kiyoko; Kadono-Okuda, Keiko; Kato, Yosuke; Yamamoto, Masanori; Shimabukuro, Michio; Chowdhury, Subrata; Xu, Jinhua; Choi, Su Kyung; Kataoka, Hiroshi; Suzuki, Akira; Yamakawa, Minoru

doi:10.1016/0965-1748(94)00080-2

Cited by 68 publications

(28 citation statements)

References 19 publications

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“…Produced by a wide variety of organisms as part of a non-specific immune response, these peptides are involved in the directed destruction of various microorganisms. In B. mori, six different families of antimicrobial peptides have been identified: cecropin, attacin, lebocin, moricin, goverin, and defensin (Steiner et al, 1981;Sugiyama et al, 1995;Tanaka et al, 2008;Hara et al, 1995;Kaneko et al, 2007;Kaneko et al, 2008). The induction mechanism of these genes is divided into two distinct pathways: the Toll and IMD pathways (Lemaitre et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Production of the BmCecB1 antimicrobial peptide in transgenic silkworm

Kim¹,

Kim²,

Park³

et al. 2015

International Journal of Industrial Entomology

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This peptide has antibacterial activity against several Gram-positive and Gram-negative bacteria. Bombyx mori cecropinB1(BmCecB1) is antimicrobial peptides from Bombyx mori and belongs to cecropin family. Antimicrobial peptides are important components of the innate immune systems in all living organism. To produce the BmCecB1 antimicrobial peptide, we constructed transgenic silkworm that expressed BmCecB1 gene under the control BmA3 promoter using piggyBac vector. The use of the 3xP3-driven EGFP cDNA as a marker allowed us to rapidly distinguish transgenic silkworm. Mixtures of the donor vector and helper vector were micro-injected into 600 eggs of bivoltin silkworms, Baegokjam. In total, 49 larvae (G0) were hatched and allowed to develop into moths. The resulting G1 generation consisted of 22 broods, and we selected 2 broods containing at least 1 EGFP-positive embryo. The rate of successful transgenesis for the G1 broods was 9%. We identified 9 EGFP-positive G1 moths and these were backcrossed with wild-type moths. With the aim of identifying a BmCecB1 as antimicrobial peptide, we investigated the Radical diffusion Assay (RDA) and then demonstrated that BmCecB1 possesses high antibacterial activities against Gramnegative bacteria. Recently, a germline transformation method using the GCTAGCATGCGTGTTTTAATTTTCACG-3' and reverse primer 5'-CTTGGTTCGGCTAAAGCTATACTTAAG-3') into

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Section: Discussionmentioning

confidence: 99%

Production of the BmCecB1 antimicrobial peptide in transgenic silkworm

Kim¹,

Kim²,

Park³

et al. 2015

International Journal of Industrial Entomology

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“…2) Several antimicrobial peptides, cecropin, [8][9][10] attacin, 11) lebocin, and moricin, have been reported from the silkworm, Bombyx mori. 12,13) These peptides have a broad spectrum of antimicrobial activity.…”

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confidence: 99%

Expression of Antimicrobial Peptide Genes Encoding Enbocin and Gloverin Isoforms in the Silkworm,Bombyx mori

Kaneko

Furukawa

Tanaka

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…Sterile rearing conditions for this insect need to be developed to investigate gene expression of rhinocerosin in the midguts. Strong expression of the rhinocerosin gene in the Malpighian tubules is also unique as compared with expression patterns in different tissues of other insect antibacterial proteins (Kato et al, 1993;Sugiyama et al, 1995;Chowdhury et al, 1995). The biological significance of gene expression of rhinocerosin in the Malpighian tubules remains as a question for the future.…”

Section: Discussionmentioning

confidence: 99%

Isolation, cDNA cloning and gene expression of an antibacterial protein from larvae of the coconut rhinoceros beetle, Oryctes rhinoceros

Yang

Yamamoto

Ishibashi

et al. 1998

European Journal of Biochemistry

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An antibacterial protein, designated rhinocerosin, was purified to homogeneity from larvae of the coconut rhinoceros beetle, Oryctes rhinoceros immunized with Escherichia coli. Based on the amino acid sequence of the N-terminal region, a degenerate primer was synthesized and reverse-transcriptase PCR was performed to clone rhinocerosin cDNA. As a result, a 279-bp fragment was obtained. The complete nucleotide sequence was determined by sequencing the extended rhinocerosin cDNA clone by 5′ rapid amplification of cDNA ends. The deduced amino acid sequence of the mature portion of rhinocerosin was composed of 72 amino acids without cystein residues and was shown to be rich in glycine (11.1 %) and proline (11.1%) residues. Comparison of the deduced amino acid sequence of rhinocerosin with those of other antibacterial proteins indicated that it has 77.8% and 44.6% identity with holotricin 2 and coleoptrecin, respectively. Rhinocerosin had strong antibacterial activity against E. coli, Streptococcus pyogenes, Staphylococcus aureus but not against Pseudomonas aeruginosa. Results of reverse-transcriptase PCR analysis of gene expression in different tissues indicated that the rhinocerosin gene is strongly expressed in the fat body and the Malpighian tubule, and weakly expressed in hemocytes and midgut. In addition, gene expression was inducible by bacteria in the fat body, the Malpighian tubule and hemocyte but constitutive expression was observed in the midgut.

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Characterization of a Bombyx mori cDNA encoding a novel member of the attacin family of insect antibacterial proteins

Cited by 68 publications

References 19 publications

Production of the BmCecB1 antimicrobial peptide in transgenic silkworm

Production of the BmCecB1 antimicrobial peptide in transgenic silkworm

Expression of Antimicrobial Peptide Genes Encoding Enbocin and Gloverin Isoforms in the Silkworm,Bombyx mori

Isolation, cDNA cloning and gene expression of an antibacterial protein from larvae of the coconut rhinoceros beetle, Oryctes rhinoceros

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