• 한국잠사곤충학회지
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• 제37권2호
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• pp.167-171
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• 1995

딱정벌레목 천공성 해충인 뽕나무 하늘소(Apriona germari)의 효과적인 방제를 위하여, 뽕나무 하늘소 이병충으로 부터 곤충병원 사상균을 분리하고, 위상차 현미경 및 주사전자현미경으로 관찰하였으며, PCR(polymerase chain reaction)을 이용하여 동정하였다. 뽕나무 하늘소 이병충으로 부터 분리된 곤충병원 사상균은 현미경 관찰 결과 Beauveria속의 전형적인 형태적 특성을 나타냈다. 따라서 이들의 용이한 동정을 위하여 PCR primer(5'-ACG GGC GCT C-3')를 이용한 RAPD(random amplification of polymorphic DNA) 방법으로 분석하고, B. bassiana와 B. brongniartii의 PCR 산물을 전기영동한 결과 DNA 표식자로 이용이 가능하였다. 이상의 결과로서 본 실험에서 분리·명명된 SFB-1A는 B. bassianifh, SFB-1A는 B. bassiana로, SFB-3A는 B. brongniartii로 동정되었다.

• International Journal of Industrial Entomology and Biomaterials
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• 제11권2호
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• pp.113-117
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• 2005

A chymotrpsin gene homologue was cloned from the mulberry longicorn beetle, Apriona germari. The A. germari chymotrypsin cDNA contains an ORF of 950 nucleotides capable of encoding a 283 amino acid polypeptide with a predicted molecular mass of 29151 Da and pI of 9.38. The A. germari chymotrypsin has conserved six cysteine residues and active triad formed by His, Asp and Ser. The deduced amino acid sequence of the A. germari chymotrypsin cDNA was closest in structure to the Anthonomus grandis chymotrypsin. Northern blot analysis revealed that A. germari chymotrypsin showed the midgut-specific expression.

• International Journal of Industrial Entomology and Biomaterials
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• 제9권1호
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• pp.149-153
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• 2004

Here we report the molecular cloning of a LIM protein cDNA of the CRP (cysteine-rich protein) family from the mulberry longicorn beetle, Apriona, geramri. The A. germari LIM protein cDNA contains an open reading frame of 276 bp encoding 92 amino acid residues with a calculated molecular weight of approximately 10 kDa. The A. germari LIM protein contains the cysteine-rich consensus sequence of LIM domain and the glycine-rich consensus sequence observed in cysteine-rich protein family 1 (CRP1). The potential nuclear targeting signal is retained. The deduced amino acid sequence of the A. germari LIM protein cDNA showed 81 % identity to both Bombyx mori muscle LIM protein (Mlp) and Drosophila melanogaster Mlp60A and 77% to Epiblema scudderiana Mlp. Northern blot analysis showed that A. germari LIM protein is highly expressed in epidermis and muscle, and less strongly in midgut, but not in the fat body.

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2003년도 International Symposium of Silkworm/Insect Biotechnology and Annual Meeting of Korea Society of Sericultural Science
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• pp.155-156
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• 2003

The Coleoptera is one of the most species-rich order of animals, adapted to most terrestrial and freshwater aquatic habitats. Among them, the mulberry longicom beetle, Apriona germari Hope, is widely distributed in eastern Asia and became one of the major pests of mulberry tree in Korea. To obtain genetic information on the mulberry longicorm beetle, we have constructed cDNA library from the larvae whole-body. Here, we report Apriona germari ESTs profiles determined the 5'most end of 3072 clones. (omitted)

• International Journal of Industrial Entomology and Biomaterials
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• 제3권2호
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• pp.121-126
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• 2001

A cDNA encoding a cathepsin D homologue was cloned from a cDNA library of the mulberry longicorn beetle, Apriona germari. Sequence analysis of the cDNA encoding the cathepsin D homologue of A. germari revealed that the 1,158 bp cDNA has an open reading frame of 386 amino acid residues. The deduced protein sequence of the A. germari cathepsin D homologue shows high homology with cathepsin D in insects, Aedes aegypti (68.2% amino acid similarity) and Drosophila melanogaster (67.2% amino acid similarity). Two aspartic residues and six cystein residues in the A. germari cathepsin D homologue are present at identical locations in all of the other catepsins D. Unlike cathepsins D in two insect species, A. gemari cathepsin D homologue appears to have two putative glycosylation sites, rather than one. Phylogenetic analysis revealed the A. germari cathepsin D homologue is more closely related to insect cathepsins D than to the other animal cathepsins D. Northern blot analysis suggests that A. germari cathepsin D homologue gene is expressed in most if not all, body tissues.

• International Journal of Industrial Entomology and Biomaterials
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• 제9권2호
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• pp.187-191
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• 2004

Actin is a ubiquitous and highly conserved protein found in eukaryotic organisms. In this study, we describe the cDNA cloning and mRNA expression of an actin gene from the mulberry longicorn beetle, Apriona germari. The A. germari actin cDNA is 1524 bp containing a complete 1128 bp open reading frame that encodes a polypeptide of 376 amino acid residues with a predicted molecular weight of about 41.5 kDa. The deduced amino acid sequence of the A.germari actin cDNA showed 99% protein sequence identity to Homalodisca coagulata actin, differing at only two amino acid positions, and 92-98% protein sequence identity to known insect species actins. The predicted three-dimensional structure of A. germari actin revealed the four residue hydrophobic pulg loop characteristic of the actin family. Northern blot analysis showed that A. germari actin is highly expressed in epidermis and muscle, and less strongly in midgut, but not in the fat body of A. germari larva.

• 한국응용곤충학회지
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• 제36권3호
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• pp.264-269
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• 1997

뽕나무하늘소(Apriona germari) 및 왕똥풍뎅이 (Aphodius apicalis) 사충으로부터 4종의 Bacillus thuringiensis를 분리하였다. B. thuringiensis의 편모 항원에 의한 동정 결과, 4종의 분리된 B. thuringiensis 중에서 1종은 darmstadiensis 아종으로 판명되었으나, 나머지 3종은 33종의 어느 B. thuringiensis 편모 항체와도 반응하지 않았다. 분리된 균주의 포자와 내독소 단백질 혼합물을 이용하여 뽕나무하늘소와 왕똥풍뎅이, 누에(Bombyx mori) 및 빨간집모가(Cules pipiens pallens) 유충에 대하여 생물검정한 결과, 이들 분리주들은 검정된 곤충에 대하여 독성을 갖지 않는 것으로 나타났다. 아울러 SDS-PAGE와 agarose gel electrophoresis를 이용하여 분리된 4종의 B. thuringiensis의 내독소 단백질과 plasmid DNA 패턴을 조사한 결과, darmstadiensis와 이미 보고된 20종의 무독성 B. thuringiensis와 차이를 보여 새로운 무독성 균주로 사료된다.

• International Journal of Industrial Entomology and Biomaterials
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• 제4권1호
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• pp.63-68
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• 2002

A cDNA encoding a putative member of cathepsin B of the thiol pretense superfamily was cloned from a cDNA library of the mulberry longicorn beetle, Apriona germari. Sequence analysis of the cDNA encoding the cathepsin B of A. germari (AgCatB) revealed that the 972 bp cDNA has an open reading frame of 324 amino acid residues. The deduced protein sequence of the AgCatB showed high homology with cathepsin B of the insects, Bombyx mori (47.3% amino acid identity), Helicoverpa armigera (46.6%) and Sarcophaga peregrina (45.6%), and the lowest homology with Aedes aegypti (33.2%). The AgCatB contains six disulfate bonds typical for cysteine pretenses. The three amino acid positions Cys-109, His-267, and Asn-287 which are conserved, active sites characteristic for cathepsin B, were also found. Phylogenetic analysis further confirmed that the AgCatB has a close relationship with that of B. mori, H. armigera and S. peregrina.

• International Journal of Industrial Entomology and Biomaterials
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• 제1권2호
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• pp.137-141
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• 2000

To determine effects of temperatures and photoperiods on larval development of the mulberry longicorn beetle, Apriona germari, the larvae were reared at various rearing temperatures and under the various photoperiods on an artificial diet. The larval period of A. germari was extended as long as the temperature was lowered. Also the larval development in terms of length and weight of larvae was increased. However, survival rate during larval stage significantly decreased at 15$^{\circ}C$ and $20^{\circ}C$ than at $25^{\circ}C$ and $30^{\circ}C$. The results indicated that the favorable temperature for artificial diet rearing of A. germari fell at least above $25^{\circ}C$ constantly. In photoperiod conditions, survival rate and larval development for A. germari were obviously most effective under a photoperiod of 14L:10B. As a result in artificial diet rearing of a. germari at $25^{\circ}C$ and under a photoperiod of 14L:10D was mostly favorable in terms of larval development and period.

• 한국잠사곤충학회지
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• 제41권2호
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• pp.82-86
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• 1999

Hemolymph proteins and vitellogenin from mulberry longicorn beetle, Apriona germari HOPE, were indentified, and their changed were analyzed during the larval-pupal-adult development and in the newly laid eggs. Thres major hemolymph proteins were observed in the hemolymph during the larval-pupal-adult development and the intensity of their proteins was clearly observed during the pupal stage. From SDS-[olyacrylamide gel electrophoresis analysis, molecular weights of three major hemolymph proteins were approximately 74 kDa, 78kDa and 85kDa. Vitellogenin in A. Germati appeared in the hemolymph of only abult female and is considered to be a product synthersized within 10 days after adult emergence. The molecular weight of vitellogenin was consited of a heavy subunit (165 kDa) and a light subunit (40 kDa).