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Molecular cloning of a novel cecropin-like peptide gene from the swallowtail butterfly, Papilio xuthus
  • 비영리 CC BY-NC
  • 비영리 CC BY-NC
ABSTRACT
Molecular cloning of a novel cecropin-like peptide gene from the swallowtail butterfly, Papilio xuthus
KEYWORD
Papilio xuthus , antimicrobial peptide , RT-PCR , antibacterial activity
참고문헌
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이미지 / 테이블
  • [ Fig. 1. ]  ACP45 products of annealing control primer (ACP)- based differential display PCR system from normal and immunechallenged P. xuthus larvae were visualized via 2 % agarose gel electrophoresis and ethidium bromide staining. Candidate differential expressed cDNA is indicated with arrow. The size of product was about 310 bp.
    ACP45 products of annealing control primer (ACP)- based differential display PCR system from normal and immunechallenged P. xuthus larvae were visualized via 2 % agarose gel electrophoresis and ethidium bromide staining. Candidate differential expressed cDNA is indicated with arrow. The size of product was about 310 bp.
  • [ Fig. 2. ]  Nucleotide and deduced amino acid sequences of the cDNA encoding for the cecropin-like peptide (CLP) of P. xuthus. The putative mature protein sequence is underlined and an asterisk indicates the terminated codon. The solid arrow indicates the putative cleavage sites for the signal peptide. The C-terminal acidic pro-region is highlighted in gray.
    Nucleotide and deduced amino acid sequences of the cDNA encoding for the cecropin-like peptide (CLP) of P. xuthus. The putative mature protein sequence is underlined and an asterisk indicates the terminated codon. The solid arrow indicates the putative cleavage sites for the signal peptide. The C-terminal acidic pro-region is highlighted in gray.
  • [ Fig. 3. ]  Amino acid sequence alignment among P. xuthus cecropin-like peptide (Px-CLP) precursor and other typical cecropin D precursors from lepidopteran insects. Ha-CecD, cecropin D from Helicoverpa armigera (EU041763); Am-CecD, cecropin D from Antheraea mylitta (ABG72696); Ms-Cec6, cecropin6 from Manduca sexta (CAL25128); Ar-Hinnavin II, Artogeia rapae hinnavin II (AAT94287); Ms-Bactericidin, M. sexta bactericidin (AAA29306); Hc-CecD, cecropin D from Hyalophora cecropia (AAA29186); Tn-CecD, cecropin D from Trichoplusia ni (ABV68873); Bm-CecD, cecropin D from Bombyx mori (BAA31507). Multiple sequence alignment was performed using CLUSTALW program.
    Amino acid sequence alignment among P. xuthus cecropin-like peptide (Px-CLP) precursor and other typical cecropin D precursors from lepidopteran insects. Ha-CecD, cecropin D from Helicoverpa armigera (EU041763); Am-CecD, cecropin D from Antheraea mylitta (ABG72696); Ms-Cec6, cecropin6 from Manduca sexta (CAL25128); Ar-Hinnavin II, Artogeia rapae hinnavin II (AAT94287); Ms-Bactericidin, M. sexta bactericidin (AAA29306); Hc-CecD, cecropin D from Hyalophora cecropia (AAA29186); Tn-CecD, cecropin D from Trichoplusia ni (ABV68873); Bm-CecD, cecropin D from Bombyx mori (BAA31507). Multiple sequence alignment was performed using CLUSTALW program.
  • [ Fig. 4. ]  RT-PCR analysis of P. xuthus cecropin-like peptide (Px-CLP) gene transcription in native larvae and the LPS-challenged larvae 12 h and 24 h post-injection. The gene for Actin was used as a control.
    RT-PCR analysis of P. xuthus cecropin-like peptide (Px-CLP) gene transcription in native larvae and the LPS-challenged larvae 12 h and 24 h post-injection. The gene for Actin was used as a control.
  • [ Fig. 5. ]  The schemes of synthetic Px-CLPa with a 37-residue (theoretical mass of 4018.59) and Px-CLPb with a 44-residue (theoretical mass of 4850.34). Charged residues are indicated by + or ? above the amino acid sequences. Hydrophobic residues are in red, hydrophobic residues on the same surface are underlined.
    The schemes of synthetic Px-CLPa with a 37-residue (theoretical mass of 4018.59) and Px-CLPb with a 44-residue (theoretical mass of 4850.34). Charged residues are indicated by + or ? above the amino acid sequences. Hydrophobic residues are in red, hydrophobic residues on the same surface are underlined.
  • [ Fig. 6. ]  Radial diffusion assays for antibacterial activity of synthetic Px-CLPa and Px-CLPb against E. coli ML35. The analyzed samples were introduced as a series of five serial two-fold dilution (concentration from 200 to 6.25 μg/mL). Bacteria were grown overnight at 37 ℃.
    Radial diffusion assays for antibacterial activity of synthetic Px-CLPa and Px-CLPb against E. coli ML35. The analyzed samples were introduced as a series of five serial two-fold dilution (concentration from 200 to 6.25 μg/mL). Bacteria were grown overnight at 37 ℃.
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