Sucrose hydrolases from the midgut of the sugarcane stalk borer Diatraea saccharalis

Carneiro, Cíntia N.B.; Isejima, Eliza Mitiko; Samuels, Richard Ian; Silva, Carlos P.

doi:10.1016/j.jinsphys.2004.09.011

Cited by 23 publications

(26 citation statements)

References 11 publications

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“…No other b-fructofuranosidase gene has been found in the S. levis transcriptome, but two different b-fructofuranosidase genes are reported for the D. ponderosae genomic database. bfructofuranosidase genes have been described in species of Lepidoptera and more than one gene has been found in B. mori, Diatraea saccharalis and M. sexta (Daimon et al, 2008;Carneiro et al, 2004;Pauchet et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Beta-fructofuranosidases have been widely described in microorganisms, but were not known in the animal kingdom until very recently, when found in the order Lepidoptera (Santos and Terra, 1986;Sumida et al, 1994;Carneiro et al, 2004). The first reports on the occurrence of transcripts encoding b-fructofuranosidase in animals were in a midgut cDNA library of Helicoverpa armigera larvae (Pauchet et al, 2008) as well as Bombyx mori, in which the enzyme was characterized and immunolocalized in the midgut and silk gland of larvae (Daimon et al, 2008).…”

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confidence: 99%

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A novel β-fructofuranosidase in Coleoptera: Characterization of a β-fructofuranosidase from the sugarcane weevil, Sphenophorus levis

Pedezzi

Fonseca

Júnior

et al. 2014

Insect Biochemistry and Molecular Biology

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

A novel β-fructofuranosidase in Coleoptera: Characterization of a β-fructofuranosidase from the sugarcane weevil, Sphenophorus levis

Pedezzi

Fonseca

Júnior

et al. 2014

Insect Biochemistry and Molecular Biology

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“…If the genes are present in other insects that do not feed on mulberry leaves, such as S. cynthia, comparative studies on their enzymatic properties, expressions, and localizations would provide further clues into the silkworm's ability to circumvent the mulberry's defense system. Since previous reports have described several insect sucrases that exhibited a kinetic property characteristic of a ␤-fructofuranosidase (10,13), it is probable that ␤-fructofuranosidase genes exist in other insects too. We are currently conducting 3 T. Shimada, T. Daimon, T. Taguchi, and K. Mita, unpublished data.…”

Section: Discussionmentioning

confidence: 99%

β-Fructofuranosidase Genes of the Silkworm, Bombyx mori

Daimon

Taguchi

Meng

et al. 2008

Journal of Biological Chemistry

106

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Mulberry latex contains extremely high concentrations of alkaloidal sugar mimic glycosidase inhibitors, such as 1,4-dideoxy-1,4-imino-D-arabinitol (D-AB1) and 1-deoxynojirimycin (DNJ).Although these compounds do not harm the silkworm, Bombyx mori, a mulberry specialist, they are highly toxic to insects that do not normally feed on mulberry leaves. D-AB1 and DNJ are strong inhibitors of ␣-glucosidases (EC 3.2.1.20); however, they do not affect the activity of ␤-fructofuranosidases (EC 3.2.1.26). Although ␣-glucosidase genes are found in a wide range of organisms, ␤-fructofuranosidase genes have not been identified in any animals so far. In this study, we report the identification and characterization of ␤-fructofuranosidase genes (BmSuc1 and BmSuc2) from B. mori. The BmSuc1 gene was highly expressed in the midgut and silk gland, whereas the expression of BmSuc2 gene was not detected. BmSuc1 encodes a functional ␤-fructofuranosidase, whose enzymatic activity was not inhibitedbyDNJorD-AB1.WealsoshowedthatBmSUC1proteinlocalized within the midgut goblet cell cavities. Collectively, our data clearly demonstrated that BmSuc1 serves as a sugar-digesting enzyme in the silkworm physiology. This anomalous presence of the ␤-fructofuranosidase gene in the B. mori genome may partly explain why the silkworm can circumvent the mulberry's defense system.Certain plants have evolved defense mechanisms against insect predation through the production of defense compounds (1-3). This is reflected by the limited number of insects capable of feeding on such plants. In particular, plant latex often contains a wide variety of toxic compounds, such as alkaloids and proteases, which play an important role in a plant's defense mechanism against insect herbivory (2, 4 -6).Mulberry latex contains extremely high concentrations of alkaloidal sugar mimic glycosidase inhibitors, such as 1,4-2 1-deoxynojirimycin (DNJ), and 1,4-dideoxy-1,4-imino-D-ribitol (2, 7). These sugar mimic alkaloids are not toxic to larvae of the silkworm Bombyx mori (family Bombycidae), which feed only on mulberry leaves and have been reared on them for thousands of years (2). However, these compounds are highly toxic to other caterpillars, such as the eri-silkworm Samia cynthia ricini (family Saturniidae) and cabbage moth Mamestra brassicae (family Noctuidae), for which mulberry trees are not the host plant in natural conditions (2). This indicates that the silkworm has evolved an unknown mechanism to circumvent the toxic effects of such sugar mimic alkaloids, thus enabling it to feed and grow well on mulberry leaves (2, 8).Sucrases are digestive enzymes that hydrolyze ␣-glucosyl (␣-glucosidase, EC 3.2.1.20) or ␤-fructosyl residue (␤-fructofuranosidase, EC 3.2.1.26) of the substrate. D-AB1 and DNJ are strong inhibitors of ␣-glucosidases; however, they do not exhibit inhibitory activity against ␤-fructofuranosidases (7). Although ␣-glucosidases are found in many types of organisms, including bacteria, fungi, plants, and animals, it has been generally assumed that ␤-fructof...

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“…Insect midgut sucrase has been identified as either a soluble enzyme or being associated with the membrane. It is generally thought that insect sucrase activity depends mainly on a-glucosidases Carneiro et al, 2004). On the other hand, several studies have reported the occurrence of b-fructofuranosidase in lepidopteran insects (Santos and Terra, 1986;Sumida et al, 1994a;Carneiro et al, 2004;Daimon et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…It is generally thought that insect sucrase activity depends mainly on a-glucosidases Carneiro et al, 2004). On the other hand, several studies have reported the occurrence of b-fructofuranosidase in lepidopteran insects (Santos and Terra, 1986;Sumida et al, 1994a;Carneiro et al, 2004;Daimon et al, 2008). Although a large variety of a-glucosidase genes have been recently identified in Diptera (Ferreira et al, 2010;Gabrisko and Janecek, 2011;Gabrisko, 2013;Zhang et al, 2013), there are only a few studies on a-glucosidase genes of Lepidoptera.…”

Section: Introductionmentioning

confidence: 99%

A novel sucrose hydrolase from the bombycoid silkworms Bombyx mori, Trilocha varians, and Samia cynthia ricini with a substrate specificity for sucrose

Wang

Kiuchi

Katsuma

et al. 2015

Insect Biochemistry and Molecular Biology

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Sucrose hydrolases from the midgut of the sugarcane stalk borer Diatraea saccharalis

Cited by 23 publications

References 11 publications

A novel β-fructofuranosidase in Coleoptera: Characterization of a β-fructofuranosidase from the sugarcane weevil, Sphenophorus levis

A novel β-fructofuranosidase in Coleoptera: Characterization of a β-fructofuranosidase from the sugarcane weevil, Sphenophorus levis

β-Fructofuranosidase Genes of the Silkworm, Bombyx mori

A novel sucrose hydrolase from the bombycoid silkworms Bombyx mori, Trilocha varians, and Samia cynthia ricini with a substrate specificity for sucrose

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