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PubMed2002

Effect of fenvalerate-20EC on sericigenous insects. I. Food utilization in the late-age larva of the silkworm, Bombyx mori L.

The effect of the common pyrethroid insecticide fenvalerate-20EC (Sumicidine-20EC) on food utilization parameters in the pure multivoltine (Pure Mysore) and pure bivoltine (NB4D2) races of silkworm, Bombyx mori, fed ad libitum with Morus alba, was studied in the final two instars. Insecticide treatment was found to reduce the rates of feeding, assimilation, and conversion along with the efficiencies of conversion of ingested and digested food into body substance. This was due to the toxic effects, which interfered with the silkworms' feeding behavior, and physiology of digestion, and the magnitude of changes increased with the increase in the concentration of fenvalerate used. To overcome the deleterious effects of such pyrethroid insecticides, it has been suggested that the safe periods for use of mulberry leaves contaminated with fenvalerate for summer and winter.

Animals↗
PubMed2002

Effect of fenvalerate-20EC on sericigenous insects. II. Digestive enzymes in the nutritive physiology of silkworm, Bombyx mori L.

Changes in the activities of a few digestive enzymes after fenvalerate-20EC treatment were studied during the late stages of multivoltine and bivoltine silkworms, Bombyx mori. Insecticide treatment induced a reduction in the activity of such enzymes as amylase, sucrase, and protease, whereas the trehalase activity was enhanced when the midgut was used as the source of enzyme. The changes recorded in the activity of these enzymes indicated probable adverse effects of fenvalerate on silkworm metabolism through interference with the functional abilities of digestive enzymes.

Amylases↗
PubMed1999

Ecdysone has an effect on the regeneration of midgut epithelial cells that is distinct from 20-hydroxyecdysone in the silkworm Bombyx mori.

We investigated the effects of two ecdysteroids, ecdysone (E) and 20-hydroxyecdysone (20E), on silkworm larval development. Silkworm larvae, Bombyx mori, were fed an artificial diet supplemented with 20E during the fourth instar to promote premature molting. At the onset of the fifth instar, these precocious fifth-instar larvae were fed diets supplemented with either E or 20E to determine the effects of the two ecdysteroids on the morphology of midgut epithelial cells. Regeneration of midgut epithelial cells normally occurs only during the molting period. However, in larvae fed E, complete replacement of midgut epithelial cells was observed 24 h before the larvae entered apolysis. In larvae fed 20E, the morphology of midgut epithelial cells was disrupted, leading to death of the larvae during the fifth instar. We also observed similar differences in the effects of the two ecdysteroids in an in vitro experiment. These results suggest that E has a specific effect on the morphological change of midgut epithelial cells in precocious fifth-instar larvae that is distinct from 20E.

Animals↗
PubMed1998

Evidence for growth of strains of the plant epiphytic bacterium Erwinia herbicola and transconjugation among the bacterial strains in guts of the silkworm Bombyx mori.

Growth of plant epiphytic bacteria Erwinia herbicola and Pseudomonas syringae in guts of the silkworm, Bombyx mori, was studied. Fifth instar silkworm larvae were fed artificial diets supplemented with these bacteria for 6 to 12 h followed by uncontaminated diets. At 1, 3, and 6 days after feeding, bacteria were isolated from insect guts and feces. A much larger population of E. herbicola was detected in the samples collected 3 and 6 days after the inoculation than in samples collected after 1 day, indicating that these bacteria grew in the insect gut, while P. syringae was unable to survive. Transconjugation between E. herbicola strains in the insect gut was also examined. First, either a donor or a recipient strain was fed to the insects in artificial diets containing the bacteria during 12 h, and then pairing strains were fed during 12 h after starvation for 12 h. The conjugative plasmid pBPW1::Tn7 was transferred into recipient cells at very high frequencies (10(-1)/recipient after 3 days and 10(-3) after 6 days) in insect guts. Indigenous plasmids of E. herbicola mobilized RSF1010 plasmid into recipient cells at frequencies of 10(-4) in insect guts. These transconjugants were detected in the feces of the insects. Thus, plasmid-mediated gene transfer among the epiphytic bacteria in insect guts was demonstrated. The results obtained suggest that in insecta gene transfer may play an important role in the evolution of plant epiphytic bacteria.

Animals↗
PubMed1995

Production of a chimeric fibroin light-chain polypeptide in a fibroin secretion-deficient naked pupa mutant of the silkworm Bombyx mori.

The allelic Nd-s and Nd-sD mutations of the silkworm Bombyx mori are mapped to the same locus as that of the fibroin light (L)-chain gene (Fib-L). The silkworm carrying the homozygous Nd-s or Nd-sD mutation secretes less than 0.3% of the normal level of fibroin and produces a thin cocoon (naked pupa). In this study, cDNA sequences of the Nd-s and Nd-sD L-chains were compared with the cDNA and genomic sequences of the L-chain of the B. mori J-139 strain, a normal-level producer of fibroin. The two mutant cDNA sequences are almost identical except for one base change in the coding region. The N-terminal half of the L-chain encoded by exons I to III is identical between the mutants and J-139, but the rest of the molecule is completely different. The C-terminal half of the Nd-sD mutant L-chain is encoded by two exons, IV' and V', which are brought into proximity with the exon III by recombination between sequences in the third intron and in the far downstream region with concomitant loss of a region containing exons IV to VII. Sequences corresponding to exons IV' and V' are present about 10 kb downstream of the L-chain gene in the J-139 genome. Their homologous sequences have not been found in the DNA and protein databases. The chimeric L-chain molecule of about 27 kDa is present in posterior silk glands of Nd-s and Nd-sD strains without disulfide-bonding to the fibroin heavy (H-) chain, as revealed by Western blotting with the antibody specific to the C-terminal half of the mutant L-chain.

Amino Acid Sequence↗
PubMed1993

Preferential extrachromosomal localization of exogenous DNA in transgenic silkworm Bombyx mori L.

Transgenic silkworms (Bombyx mori L.) were obtained by microinjection of plasmid pPrC-LTR1.5, which carris 1.5 DNA copies of Rous sarcoma virus (RSV) long terminal repeats (LTRs) inserted in the vector pBR322. The transgene was transmitted over the three generations obtained up to now. Most of the exogenous DNA failed to integrate into the genome and persisted as an extrachromosomal element that is subject to rearrangements. Plasmids carrying only part of the input DNA together with fragments of silkworm DNA were rescued from the transgenic animals. One of the rescued plasmids contained a sequence which belongs to a family of evolutionarily conserved repeated sequences.

Animals↗
PubMed1981

Genetics of insect hemolymph beta-N-acetylglucosaminidase in the silkworm, Bombyx mori.

The distribution of insect hemolymph beta-N-acetylglucosaminidase was investigated in the silkworm, Bombyx mori. Activity in 115 varieties was 6.92 +/- 3.22 units/ml, ranging from 1.4 to 17.0 units/ml. No enzyme-deficient individuals were observed. By selecting individuals showing either high or low enzyme activities, homozygotes were separated with activities varying 10-fold between isolates. No differences in activity of alpha-mannosidase and beta-galactosidase were observed. Thus, it appears that high- or low-enzyme silkworms (High or Low lines) shared the same genetic background except for the gene concerning the activity of beta-N-acetylglucosaminidase. Studies on the heredity of the enzyme indicated that the synthesis of the enzyme protein was controlled by an autosomal allele. Examination by immunotitration and CM52-cellulose column chromatography revealed that the difference in activity between High and Low lines was due to the amount of the active enzyme, but not to an endogeneous activator or inhibitor. Furthermore, there was no isozymic difference in beta-N-acetylglucosaminidase. Slab gel electrophoresis on polyacrylamide showed a species of enzyme (A) that stained more intensely in the High line. For the second species of enzyme (B), the converse was true. This evidence suggests that enzyme levels in hemolymph are under the control of a gene affording association of enzyme subunits to the active enzyme molecule.

Acetylglucosaminidase↗
PubMed1983

Genetics of insect hemolymph alpha-mannosidase in the silkworm, Bombyx mori.

The genetics of hemolymph alpha-mannosidase was investigated in the silkworm, Bombyx mori. By selecting individuals showing either high or low enzyme activities, homozygotes were separated, with activities varying about five-fold. No differences in the activities of beta-galactosidase and beta-N-acetylglucosaminidase were observed. Thus, it seems that high- and low-enzyme silkworms (High and Low Lines) share the same genetic background except for the gene concerning the activity of alpha-mannosidase. The synthesis of the enzyme is controlled by an autosomal allele. Furthermore, expression of the gene varies from tissue to tissue, and there is no correlation between enzyme activity and growth rate. The difference in activity between High and Low lines is due to the amount of active enzyme, not to an endogeneous activator or inhibitor. There was no isozymic difference in alpha-mannosidase.

Alleles↗
PubMed1984

Genetic variants of protease inhibitors against fungal protease and alpha-chymotrypsin from hemolymph of the silkworm, Bombyx mori.

Many electrophoretic variants of hemolymph inhibitors of proteases from Aspergillus melleus and pancreatic alpha-chymotrypsin were found using 126 silkworm strains. Six inhibitors of the fungal protease were detected and eight of chymotrypsin; the distribution of inhibitors among Japanese, Chinese, and European races was investigated. Comparison of electrophoretic patterns from F1 hybrids and parents showed that the offspring produce inhibitors of both parental types. Segregation in F2 and backcrossing suggest that the expression of each inhibitor is controlled in most cases by a pair of alleles which are responsible for strong and null bands. Two bands of fungal protease inhibitors C and D were controlled by codominant alleles. These results suggest that polymorphism of hemolymph protease inhibitors in the silkworm would be a useful experimental system for the study of the genetic control of protease inhibitors.

Animals↗
PubMed1990

The effect of low level ionizing radiation on embryogenesis of silkworm, Bombyx mori L.

The effect of chronic radiation, 100, 1000 and 4000 times exceeding the natural background radiation, on embryogenesis of silkworm, Bombyx mori has been investigated. It is shown that low level ionizing radiation shortens by several hours the period of embryogenesis while the larva mass increases as the development proceeds. A single preincubational exposure of silkworm eggs to a dose of 2 Gy increases the mass of larvae as well as the cocoon shell weight, silk-bearing and the raw silk production.

Animals↗
PubMed1992

High level expression of a frog alpha-amidating enzyme, AE-II, in cultured cells and silkworm larvae using a Bombyx mori nuclear polyhedrosis virus expression vector.

A Xenopus laevis peptidyl C-terminal alpha-amidating enzyme (AE-II) gene, modified by deletion of a region encoding the putative membrane-spanning domain and the putative C-terminal cytosolic tail, was expressed in BoMo-15 AIIc insect cells and silkworm larvae using a Bombyx mori baculovirus expression vector system. The expressed enzyme was identified predominantly in the culture medium and the hemolymph of silkworm larvae, indicating successful secretion of the expressed AE-II. The level of recombinant enzyme in the larval hemolymph at 4 days post-infection (40 micrograms/ml) was more than 100-fold the peak levels found in the culture medium (250 ng/ml). The enzyme activity in the larval hemolymph at 4 days post-infection was 3700 units/ml.

Animals↗
PubMed2004

Targeting of human aFGF gene into silkworm, Bombyx mori L. through homologous recombination.

The long-arm and short-arm genes of fibroin light chain (L-chain) of silkworm, Bombyx Mori L., and the gene of human acidic fibroblast growth factor were cloned respectively and subsequently inserted into a transfer vector pVL1392 used as a tool to target the L-chain region of the silkworm genome. Genomic DNA from their offsprings was extracted and the expected targeting was detected using polymerase chain reaction and DNA sequencing, as well as protein analysis. The results showed that positive events occurred and that the FGF gene was integrated into the L-chain locus through homologous recombination.

Animals↗
PubMed2005

Expression of porcine lactoferrin by using recombinant baculovirus in silkworm, Bombyx mori L., and its purification and characterization.

Lactoferrin is a multifunctional glycoprotein that is present in several mucosal secretions. In this study, we exploited the silkworm, Bombyx mori, as host for the recombinant baculovirus harboring the porcine lactoferrin (PLF) gene to produce the recombinant PLF (rPLF). Around 205 mug of rPLF was purified from a single silkworm pupa infected by the virus and the rPLF was proved to be biologically active. This method established in our study will pave the way for efficient industrial production of rPLF on a large scale for further utilization of this protein as a feed additive in the future.

Animals↗
PubMed2003

Classification of larval circulating hemocytes of the silkworm, Bombyx mori, by acridine orange and propidium iodide staining.

Circulating hemocytes of the silkworm can be classified by fluorescence microscopy following staining with acridine orange and propidium iodide. Based on their fluorescence characteristics, three groups of circulating hemocytes can be distinguished. The first group, granulocytes and spherulocytes, is positive for acridine orange and contain bright green fluorescent granules when observed by fluorescence microscopy. In granulocytes, these green granules are heterogeneous and relatively small. In contrast, in spherulocytes, the green granules appear more homogenous and larger. The second group of hemocytes consists of prohemocytes and plasmatocytes. These cells appear faint green following staining with acridine orange and do not contain any green fluorescent granules in the cytoplasm. Prohemocytes are round, and their nuclei are dark and clear within a background of faint green fluorescence. Inside the nucleus there are one or two small bright green fluorescent bodies. Plasmatocytes are irregularly shaped and their nuclei are invisible. Oenocytoids belong to the third group, and their nuclei are positive for propidium iodide. Therefore, all five types of circulating hemocytes of the silkworm, including many peculiar ones that are difficult to identify by light microscopy, can now be easily classified by fluorescence microscopy following staining with acridine orange and propidium iodide. In addition, we show that hemocytes positive for acridine orange and propidium iodide are in fact living cells based on assays for hemocyte composition, phagocytosis, and mitochondrial enzyme activity.

Acridine Orange↗
PubMed2002

Characterization of the kynurenine 3-monooxygenase gene corresponding to the white egg 1 mutant in the silkworm Bombyx mori.

Kynurenine 3-monooxygenase (KMO, EC 1.14.13.9), which catalyzes the oxidation of kynurenine to 3-hydroxykynurenine, is involved in the synthesis of ommochrome pigments in insects. A silkworm mutant, white egg 1 ( w-1), has been shown to be deficient in this enzyme activity. The mutant is characterized morphologically by its white eyes and the fact that the females lay white eggs. To analyze the relationship between the KMO gene and the mutation, we first determined the entire sequence of a full-length 2.0-kb cDNA and examined its expression pattern in the wild type. The cDNA sequence contains one ORF encoding a polypeptide of 456 amino acids, and transcripts were detected in the larval Malpighian tubules and the pupal ovaries, but not in other tissues. Southern analysis and nucleotide sequencing showed that the KMO gene is present in a single copy and consists of ten exons distributed over a 16-kb region. Comparison of the transcripts between the wild type and mutant silkworms showed that the wild type expressed a single transcript, whereas the mutant exhibited markedly reduced amounts of two transcripts with sizes of 2.0 kb and 1.8 kb. Nucleotide sequence analysis of these mutant transcripts indicated that sequences corresponding to the ninth and tenth exons were missing. Inverse PCR and Southern analysis of the mutant gene demonstrated that the corresponding genomic region was deleted in the w-1 mutant.

Amino Acid Sequence↗
PubMed2005

Site-specific gene integration in cultured silkworm cells mediated by phiC31 integrase.

The integrase from the Streptomyces bacteriophage phiC31 carries out efficient recombination between an attP site in the phage genome and an attB site in the host chromosome. In the present study, we have used the phiC31 integrase system to mediate site-specific recombination in the cultured silkworm cell line BmN4. A plasmid containing a cDNA encoding DsRed flanked by two phiC31 attP sites was co-transfected together with a helper plasmid encoding the phiC31 integrase into a cell line in which phiC31 attB sites inserted between a baculovirus IE2 promoter, and a polyadenylation signal are present in one chromosome. Seven days after transfection, expression of DsRed was observed in transformed cells. Nucleotide sequence analysis demonstrated that the expected recombination between the attB and attP sites had been precisely carried out by the phiC31 integrase. These results indicate that the phiC31 site-specific recombination system should be widely applicable for efficient site-specific gene integration into silkworm chromosomes.

Animals↗
PubMed2000

Identification and characterisation of a silkworm ABC transporter gene homologous to Drosophila white.

In the silkworm, Bombyx mori, many eye- and egg-colour mutations affecting the synthesis and accumulation of ommochrome pigments have been described. In order to understand the pigment precursor transporters involved, ABC transporter genes homologous to the Drosophila white gene were isolated from the silkworm. Reverse transcriptase-polymerase chain reactions (RT-PCR) using embryonic mRNA amplified three cDNA fragments, named Bmwh1, Bmwh2 and Bmwh3 that showed homology to the white gene. Since Bmwh3 shows the highest degree of sequence identity and a similar expression pattern to the Drosophila homologue, we characterised this gene further. A 2667-bp Bmwh3 cDNA isolated from an embryonic library has one ORF encoding a polypeptide of 687 amino acids. The predicted protein has one ATP-binding domain, six transmembrane-spanning segments and high similarity to the Drosophila WHITE protein. Southern analysis indicates that Bmwh3 is a single-copy gene. Polyadenylated Bmwh3 transcripts about 2.7 kb long were detected in eggs, Malpighian tubules and pupal heads, but not in testes, posterior silk glands or fat body cells. The level of Bmwh3 mRNA was reduced in w3 and w3ol mutants but normal in other egg- and eye-colour mutants, suggesting that Bmwh3 correspond to the w3 locus. Genetic analysis was used to map the cloned gene to chromosome 10.

ATP-Binding Cassette Transporters↗
PubMed2001

Syntheses of glycine and L-serine by their interconversion in the posterior silkgland of the silkworm, Bombyx mori.

It was observed by solution-state 13C NMR spectroscopy that a great portion of the 13C of [1-13C]L-serine fed to the 5th instar larvae of the silkworm, Bombyx mori was incorporated into C1 of glycine in silk fibroin. [1-13C]Glycine was detected along with [1-13C]serine in fibroin of the posterior silkgland cultured in a medium containing [1-13C]serine. This formation of [1-13C]glycine was inhibited by addition of aminopterin to the culture medium. These findings suggest that an active conversion from serine to glycine, which needs tetrahydrofolate, occurs in the posterior silkgland for fibroin synthesis. Moreover, the solid-state 13C CP/MAS spectrum of the fibroin prepared from cocoons spun by larvae fed with [13C]formate revealed that serine C3 was labelled specifically with 13C, suggesting that the reverse conversion from glycine to serine took place in the silkworm. The posterior silkgland has the ability to synthesize not only fibroin but also its major materials, glycine and serine.

Animals↗