Bombyx mori

Average wing-hinge Prealar arm Collagen (oxhide) Elastin (ox ligamentum nuchae) Silk fibroin Bombyx mori)... 

Other eukaryotes included Apis mellifera, Bombyx mori, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Tetraodon nigroviridis. 

Andersen et al. (1996) and Andersen (1995) have studied the effect of temperature on the recombinant protein production using a baulovinis/insect cell expression system. In Tables 17.15, 17.16, 17.17, 17.18 and 17.19 we reproduce the growth data obtained in spinner flasks (batch cultures) using Bombyx mori (Bm5) cells adapted to serum-free media (Ex-Cell 400). The working volume was 125 ml and samples were taken twice daily. The cultures were carried out at six different incubation temperatures (22, 26,28, 30 and 32 TT). 

Silk. Silk, the only natural fiber that comes in filament form, has been and still is one of the most appreciated and valued textile fibers. Silk filaments are secreted by the larvae of several types of silk moths to make their cocoons. Most silk is derived, however, from the larvae of the Bombyx mori moth, which has been widely cultivated in China for over 5000 years. Fragments of silk fabric dated to the late fourth millennium b.c.e. were found at Qianshanyang, in the province of Zhejiang, in China. There are, however, even earlier indications of the use of silk silk remains were found together with an eleventh-century b.c.e. mummy in Egypt, probably also providing evidence of ancient trading routes between the Far and Middle East. 

The larvae of Bombyx mori, the cultivated moth from which most silk has long been and still is made, feed on leaves of mulberry trees. In addition to cultivated silk, small quantities of "wild silk," also known as nonmulberry silk, have been derived in many parts of the world from the cocoons of moths other than Bombyx mori. Table 90 lists wild silks and the insect species that produce them (Peigler 1993 Jolly et al. 1979). 

Z. E. Jouni and M. Wells, Purification of a carotenoid-binding protein from the midgut of the silkworm, Bombyx mori, Ann. N. Y. Acad. Sci. 691 (1993) 210-212. 

Fujii, H., Morooka, J., Tochihara, S., Kawaguchi, Y., and Sakaguchi, B. 1988a. Existence of carotenoids binding protein in larval hemolymph of the yellow blood strain of Bombyx mori. J. Seric. Sci. Jpn., 57(2) 94-99. 

Gopalapillai, R., Kadono-Okuda, K., Tsuchida, K. et al. 2006. Lipophorin receptor of Bombyx mori cDNA cloning, genomic structure, alternative splicing, and isolation of a new isoform. J. Lipid Res., 47(5) 1005-1013. 

Hara, W., Sosnicki, S., and Banno, Y. et al. 2007. Mapping analysis of carotenoid-binding protein of Bombyx mori by restriction fragment length polymorphism. J. Insect Biotechnol. Sericol., 76(3) 149-154. 

Imamura, M., Nakai, J., Inoue, S., Quan, G. X., Kanda, T., and Tamura, T. 2003. Targeted gene expression using the GAL4/UAS system in the silkworm Bombyx mori. Genetics, 165(3) 1329-1340. 

Jouni, Z. E. and Wells, M. A. 1996. Purification and partial characterization of a lutein-binding protein from the midgut of the silkworm Bombyx mori. J. Biol. Chem., 271(25) 14722-14726. 

Sakudoh, T., Tsuchida, K., and Kataoka, H. 2005. BmStartl, a novel carotenoid-binding protein isoform from Bombyx mori, is orthologous to MLN64, a mammalian cholesterol transporter. Biochem. Biophys. Res. Commun., 336(4) 1125—1135. 

Suetsugu, Y., Minami, H., Shimomura, M. et al. 2007. End-sequencing and characterization of silkworm (Bombyx mori) bacterial artificial chromosome libraries. BMC Genomics, 8 314. 

Tabunoki, H., Sugiyama, H., Tanaka, Y. et al. 2002. Isolation, characterization, and cDNA sequence of a carotenoid binding protein from the silk gland of Bombyx mori larvae. J. Biol. Chem., 277(35) 32133-32140. 

Tabunoki, H., Higurashi, S., Ninagi, O. et al. 2004. A carotenoid-binding protein (CBP) plays a crucial role in cocoon pigmentation of silkworm (Bombyx mori) larvae. FEBS Lett., 567(2-3) 175-178. 

Tamura, T., Thibert, C., Royer, C. et al. 2000. Germline transformation of the silkworm Bombyx mori L. using apiggyBac transposon-derived vector. Nat. Biotechnol., 18(1) 81—84. 

Toyama, K. 1912. On the varying dominance of certain white breeds of the silk-worm, Bombyx mori, L. Mol. Genet. Genomics, 7(l) 252-288. 

Tsuchida, K., Soulages, J. L., Moribayashi, A., Suzuki, K., Maekawa, H., and Wells, M. A. 1997. Purification and properties of a lipid transfer particle from Bombyx mori Comparison to the lipid transfer particle from Manduca sexta. Biochim. Biophys. Acta, 1337(l) 57-65. 

Tsuchida, K., Arai, M., Tanaka, Y. et al. 1998. Lipid transfer particle catalyzes transfer of carotenoids between lipophorins of Bombyx mori. Insect Biochem. Mol. Biol., 28(12) 927-934. 

Tsuchida, K., Jouni, Z. E., Gardetto, J. et al. 2004a. Characterization of the carotenoid-binding protein of the Y-gene dominant mutants of Bombyx mori. J. Insect Physiol., 50(4) 363-372. 

Tsuchida, K., Katagiri, C., Tanaka, Y. et al. 2004b. The basis for colorless hemolymph and cocoons in the Y-gene recessive Bombyx mori mutants A defect in the cellular uptake of carotenoids. J. Insect Physiol., 50(10) 975-983. 

Uchino, K., Imamura, M., Sezutsu, H. et al. 2006. Evaluating promoter sequences for trapping an enhancer activity in the silkworm Bombyx mori. J. Insect Biotechnol. Sericology, 75 89-97. 

Normal transmission IRLD can also be used to characterize polymeric fibers, although scattering can induce sloping baselines. Raman spectroscopy then becomes a convenient alternative. Rutledge et al. have recently probed the orientation in electrospun nanofibers composed of a core of Bombyx mori fibroin and an outer shell of poly (ethylene oxide) [24], The orientation values were low, less than 0.1, as is often the case in electrospun fibers. 

Finally, as in macro-Raman experiments, orientation-insensitive spectra can also be calculated for spectromicroscopy. A method has been developed recently for uniaxially oriented systems and successfully tested on high-density PE rods stretched to a draw ratio of 13 and on Bombyx mori cocoon silk fibers [65]. This method has been theoretically expanded to biaxial samples using the K2 Raman invariant and has proved to be useful to determine the molecular conformation in various polymer thin films [58]. 

Most of the viral vectors were constructed using (1) the Autographa californica nuclear polyhedrosis virus (AcNPV), which is able to infect moth species, Spodoptera frugiperda ovarian cell lines and, in specific conditions, Drosophila cells (2) the Bombyx mori nuclear polyhedrosis virus (BmNPV), which is able to infect silkworm cells. To broaden the range of infection of hosts, a hybrid virus was generated [118,119]. 

Kondo, A. and Maeda, S. (1991) Host range expansion by recombination of the baculoviruses Bombyx mori nuclear polyhedrosis virus and Autographa californica nuclear polyhedrosis virus. Journal of Virology, 65 (7), 3625-3632. 

Two new syntheses of bombykol (6), the female sex pheromone of the silkworm moth (Bombyx mori), were reported [22,23]. Scheme 11 shows Negishi s synthesis of 6 based on organoborane chemistry [22], and Uenishi s synthesis of 6 based on palladium and nickel catalyses is summarized in Scheme 12 [23]. Both syntheses afforded bombykol of >98% purity. 

Fig. 5 Proposed signal transduction mechanisms that stimulate the pheromone biosynthetic pathway in Helicoverpa zea and Bombyx mori. It is proposed that PBAN binds to a G protein-coupled receptor present in the cell membrane that upon PBAN binding will induce a receptor-activated calcium channel to open causing an influx of extracellular calcium. This calcium binds to calmodulin and in the case of B. mori will directly stimulate a phosphatase that will dephosphorylate and activate a reductase in the biosynthetic pathway. In H. zea the calcium-calmodulin will activate adenylate cyclase to produce cAMP that will then act through kinases and/or phosphatases to stimulate acetyl-CoA carboxylase in the biosynthetic pathway...

Fig. 6 Sequence alignment of the deduced amino acid sequence from the identified cDNA encoding PBAN and related peptides from Helicoverpa zea and Bombyx mori. The putatively expressed peptides are shown in boxes. The conserved amino acids are underlined in the B. mori sequence. Putative proteolytic posttranslational processing sites are shown in bold with glycine contributing the C-terminal amide. Sequences of PBAN-like peptides are also shown in Table 1. GenBank accession numbers H. zea - PI 1159 and B. mori - BAA05971...

---