β-Fructofuranosidase Genes of the Silkworm, Bombyx mori

Daimon, Takaaki; Taguchi, Tomohiro; Meng, Yan; Katsuma, Susumu; Mita, Kazuei; Shimada, Toru

doi:10.1074/jbc.m709350200

Cited by 107 publications

(73 citation statements)

References 29 publications

(38 reference statements)

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“…B. mori acquired the first gene from a bacterium or an ancestral baculovirus and the latter gene from a bacterium [8,9]. The results suggested that both genes bestow a clear selective advantage to B. mori .…”

Section: Resultsmentioning

confidence: 99%

Horizontal gene transfer in silkworm, Bombyx mori

et al. 2011

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BackgroundThe domesticated silkworm, Bombyx mori, is the model insect for the order Lepidoptera, has economically important values, and has gained some representative behavioral characteristics compared to its wild ancestor. The genome of B. mori has been fully sequenced while function analysis of BmChi-h and BmSuc1 genes revealed that horizontal gene transfer (HGT) maybe bestow a clear selective advantage to B. mori. However, the role of HGT in the evolutionary history of B. mori is largely unexplored. In this study, we compare the whole genome of B. mori with those of 382 prokaryotic and eukaryotic species to investigate the potential HGTs.ResultsTen candidate HGT events were defined in B. mori by comprehensive sequence analysis using Maximum Likelihood and Bayesian method combining with EST checking. Phylogenetic analysis of the candidate HGT genes suggested that one HGT was plant-to- B. mori transfer while nine were bacteria-to- B. mori transfer. Furthermore, functional analysis based on expression, coexpression and related literature searching revealed that several HGT candidate genes have added important characters, such as resistance to pathogen, to B. mori.ConclusionsResults from this study clearly demonstrated that HGTs play an important role in the evolution of B. mori although the number of HGT events in B. mori is in general smaller than those of microbes and other insects. In particular, interdomain HGTs in B. mori may give rise to functional, persistent, and possibly evolutionarily significant new genes.

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Section: Resultsmentioning

confidence: 99%

Horizontal gene transfer in silkworm, Bombyx mori

et al. 2011

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“…Until recently, b-fructofuranosidases were thought to be absent from animals despite being found among bacteria, fungi, and plants. However, pairs of these proteins have been identified in several lepidopteran species, apparently having arisen via horizontal transfer from bacteria (Daimon et al, 2008). Previously, these b-fructofuranosidases have primarily been associated with larval gut, so their presence in adult saliva is consistent with a role in digestion but also marks a distinct expansion of their known functional milieu.…”

Section: Carbohydrate Hydrolysismentioning

confidence: 96%

Pollen feeding proteomics: Salivary proteins of the passion flower butterfly, Heliconius melpomene

Harpel

Cullen

Ott

et al. 2015

Insect Biochemistry and Molecular Biology

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While most adult Lepidoptera use flower nectar as their primary food source, butterflies in the genus Heliconius have evolved the novel ability to acquire amino acids from consuming pollen. Heliconius butterflies collect pollen on their proboscis, moisten the pollen with saliva, and use a combination of mechanical disruption and chemical degradation to release free amino acids that are subsequently re-ingested in the saliva. Little is known about the molecular mechanisms of this complex pollen feeding adaptation. Here we report an initial shotgun proteomic analysis of saliva from Heliconius melpomene. Results from liquid-chromatography tandem mass-spectrometry confidently identified 31 salivary proteins, most of which contained predicted signal peptides, consistent with extracellular secretion. Further bioinformatic annotation of these salivary proteins indicated the presence of four distinct functional classes: proteolysis (10 proteins), carbohydrate hydrolysis (5), immunity (6), and "housekeeping" (4). Additionally, six proteins could not be functionally annotated beyond containing a predicted signal sequence. The presence of several salivary proteases is consistent with previous demonstrations that Heliconius saliva has proteolytic capacity. It is likely that these proteins play a key role in generating free amino acids during pollen digestion. The identification of proteins functioning in carbohydrate hydrolysis is consistent with Heliconius butterflies consuming nectar, like other lepidopterans, as well as pollen. Immune-related proteins in saliva are also expected, given that ingestion of pathogens is a likely route to infection. The few "housekeeping" proteins are likely not true salivary proteins and reflect a modest level of contamination that occurred during saliva collection. Among the unannotated proteins were two sets of paralogs, each seemingly the result of a relatively recent tandem duplication. These results offer a first glimpse into the molecular foundation of Heliconius pollen feeding and provide a substantial advance towards comprehensively understanding this striking evolutionary novelty.

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“…A common feature of cuticle and silk gland is that both of them have a chitin layer. Chitin and chitin‐binding cuticular proteins together form the chitin layer, which improves the defense ability of insects but at the same time limit their growth . The renewing of the chitin layer in the cuticle is well known, but the renewing of the chitin layer in the silk gland remains unclear.…”

Section: Introductionmentioning

confidence: 99%

Comparative Proteome Analysis Reveals that Cuticular Proteins Analogous to Peritrophin‐Motif Proteins are Involved in the Regeneration of Chitin Layer in the Silk Gland of Bombyx mori at the Molting Stage

et al. 2018

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The silk gland of silkworm produces silk proteins during larval development. Many studies have long focused on the silk gland of the fifth instar larvae, but few have investigated this gland at other larval stages. In the present study, the silk gland proteomes of the fourth instar and fourth molt are analyzed using liquid chromatography-tandem mass spectrometry. In total, 2654 proteins are identified from the silk gland. A high abundance of ribosomal proteins and RR-motif chitin-binding proteins is identified during day 2 of the fourth instar (IV-2) larval developmental stage, and the expression of cuticular proteins analogous to peritrophin (CPAP)-motif chitin-binding proteins is higher during the fourth molt (IV-M). In all, nine enzymes are found to be involved in the chitin regeneration pathway in the silk gland. Among them, two chitinase and two chitin deacetylases are identified as CPAP-motif proteins. Furthermore, the expression of CPAP3-G, the most abundant CPAP-motif cuticular protein in the silk gland during the IV-M stage, is investigated using western blot and immunofluorescence analyses; CPAP3-G shows a reverse changing trend with chitin in the silk gland. The findings of this study suggest that CPAP-motif chitin-binding proteins are involved in the degradation of the chitin layer in the silk gland. The data have been deposited to the ProteomeXchange with identifier PXD008677.

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β-Fructofuranosidase Genes of the Silkworm, Bombyx mori

Cited by 107 publications

References 29 publications

Horizontal gene transfer in silkworm, Bombyx mori

Horizontal gene transfer in silkworm, Bombyx mori

Pollen feeding proteomics: Salivary proteins of the passion flower butterfly, Heliconius melpomene

Comparative Proteome Analysis Reveals that Cuticular Proteins Analogous to Peritrophin‐Motif Proteins are Involved in the Regeneration of Chitin Layer in the Silk Gland of Bombyx mori at the Molting Stage

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