• Title/Summary/Keyword: Artogeia rapae

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Control Thresholds (CTs) of Imported Cabbage Worm (Artogeia rapae L.) for Chinese Cabbage in Korea (배추에 대한 배추흰나비(Artogeia rapae L.)의 요방제수준)

  • Kwon, Min;Kim, Ju-Il;Yoon, Young-Nam;Choi, June-Yeol
    • Korean journal of applied entomology
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    • v.47 no.4
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    • pp.401-405
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    • 2008

  • This study was conducted to estimate the control thresholds (CTs) of imported cabbage worm, Artogeia rapae L., injuring Chinese cabbage. The second instar larvae of A. rapae were inoculated with five density levels on each Chinese cabbages transplanted three weeks earlier under greenhouse condition, and checked injury rates after allowing their feeding for one week and two weeks, respectively. The average leaf area consumed by single larvae was 657.7 $mm^2$ in plots inoculated at three weeks after transplanting (WAT) and 2495.8 $mm^2$ in plots at 6-WAT, respectively. In the field experiment, different numbers of A. rapae ranged from one to seven larvae were inoculated on 20 plants. The percent yield reduction (Y) of Chinese cabbage infested by different densities of A. rapae (X) for a three-week period was estimated by the following equation; (1) Y=1.764X-0.3049 ($R^2$=0.9901) in plots inoculated at 3-WAT; and (2) Y=1.0305X-0.2976 ($R^2$=0.9398) in plots inoculated at 6-WAT. Based on the relationships between the densities of A. rapae larvae and the yield index of Chinese cabbage, the number of second instar larvae which caused 5% loss of yield (gain threshold proposed by Japan), was estimated as 3.0 per 20 plants for the 3-WAT and 5.1 for the 6-WAT.

  • https://doi.org/10.5656/KSAE.2008.47.4.401 인용 PDF KSCI

Induction and Purification of Antibacterial Proteins in Larval Haemolymph of Cabbage Butterfly, Artogeja rapae (배추흰나비의 유충 혈림프로 부터 항균단백질의 유도와 분리)

  • 여성문;방인석;장병수;조은정
    • The Korean Journal of Zoology
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    • v.38 no.3
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    • pp.305-312
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    • 1995

  • The Injection of viable Escherichia coli K-12 with fifth instar larvae of cabbage butterfly, Artogeia rapae, induced at least five groups of proteins with the antibacterial activity against certain Gram-negative and/or Gram-positive bacteria in the haemolymph. These antibacterial proteins were separated and one was purified by different types of chromatography. The purified protein was heat-stable and basic peptide, and its molecular weight was approximately 4 kDa. We propose the name hinnavins for this antibacterial peptide.

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Molecular Cloning and Characterization of Lysozyme II from Artogeia rapae and its Expression in Baculovirus-infected Insect Cells

  • Bang, In-Seok;Kang, Chang-Soo
    • Animal cells and systems
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    • v.11 no.2
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    • pp.175-182
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    • 2007

  • The lysozyme II gene of cabbage butterfly Artogeia rapae was cloned from fat body of the larvae injected with E. coli and its nucleotide sequence was determined by the RACE-PCR. It has an open reading frame of 414 bp nucleotides corresponding to 138 amino acids including a signal sequence of 18 amino acids. The estimated molecular weight and the isoelectric point of the lysozyme II without the signal peptide were 13,649.38 Da and 9.11, respectively. The A. rapae lysozyme II (ARL II) showed the highest identity (81%) in the amino acid sequence to Manduca sexta lysozyme among other lepidopteran species. The two catalytic residues ($Glu^{32}$ and $Asp^{50}$) and the eight Cys residue motifs, which are highly conserved among other c-type lysozymes in invertebrates and vertebrates, are also completely conserved. A phylogenetic analysis based on amino acid sequences indicated that the ARL II was more closely related to M. sexta, Hyphantria cunea, Heliothis virescens, and Trichoplusia ni lysozymes. The ARL II gene was expressed in Spodoptera frugiperda 21 insect cells and the recombinant ARL II (rARL II) was purified from cell-conditioned media by cation exchange column chromatography and reverse phase FPLC. The purified rARL II was able to form a clear zone in lysoplate assay against Micrococcus luteus. The lytic activity was estimated to be 511.41 U/mg, 1.53 times higher than that of the chicken lysozyme. The optimum temperature for the lytic activity of the rARL II was $50^{\circ}C$, the temperature dependency of the absolute lytic activity of rARL II was higher than that of the chicken lysozyme at low temperatures under $65^{\circ}C$.

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