Identification and expression profiling of Ceratitis capitata genes coding for β-hexosaminidases

Pasini, Maria Enrica; Intra, Jari; Gomulski, Ludvik M.; Calvenzani, V.; Petroni, Katia; Briani, Federica; Perotti, M.E.

doi:10.1016/j.gene.2010.11.003

Cited by 12 publications

(11 citation statements)

References 61 publications

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“…OfHex3 belongs to class III Hexes. Although previously reported class III enzymes were involved in sperm–egg interaction [13], [14], [15], [16], this study found that OfHex3 occurred with OfHex1 in molting fluids. Enzymatic activity and expression pattern both suggested that besides functioning in fertilization, OfHex3 worked with OfHex1 in cuticle degradation.…”

Section: Introductioncontrasting

confidence: 77%

A Sperm–Plasma β-N-Acetyl-D-Hexosaminidase Interacting with a Chitinolytic β-N-Acetyl-D-Hexosaminidase in Insect Molting Fluid

Liu

Chen

et al. 2013

PLoS ONE

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Insects require molting fluids to shed the old cuticle during molting. β-N-acetyl-D-hexosaminidase, known as Hex1, together with various chitinases, is responsible for degrading the chitin component of the old cuticle. This study showed that another β-N-acetyl-D-hexosaminidase, termed OfHex3, interacted with Hex1 and functioned in the molting fluid, although the homolog of OfHex3 was known as a sperm–plasma enzyme functioning in egg–sperm recognition. OfHex3 is an enzyme cloned from the insect Asian corn borer, Ostrinia furnacalis, which is one of the most destructive pests of maize. The enzymatic activity analysis indicated that OfHex3 was able to degrade chitooligosaccharides, but at a lower rate than that of OfHex1. Because OfHex3 did not have substrate inhibition, we deduced that the presence of OfHex3 might help OfHex1 relieve substrate inhibition during chitin degradation during molting. The expression patterns of OfHex3 during O. furnacalis development were studied by real-time PCR as well as western blot. The results showed that both gene transcription and protein translation levels of OfHex3 were up-regulated during larval–larval molting. The tissue-specific expression pattern analysis indicated that OfHex3 was mostly localized in the fat body and testis. All these data further supported that Hex3 was involved in molting as well as in fertilization. This study may help to understand the complexity of cuticle degradation during insect molting, and may provide a possible target for pest control.

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Section: Introductioncontrasting

confidence: 77%

A Sperm–Plasma β-N-Acetyl-D-Hexosaminidase Interacting with a Chitinolytic β-N-Acetyl-D-Hexosaminidase in Insect Molting Fluid

Liu

Chen

et al. 2013

PLoS ONE

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“…IBS-Hexs are distributed widely in insects with the exception of the fruitfly, Drosophila melanogaster 10 and the medfly, Ceratitis capitata 11. IBS-Hexs are found to have high sequence similarity to human β- N -acetyl-D-hexosaminidases but low sequence similarity with other insect Hex enzymes.…”

Section: Introductionmentioning

confidence: 99%

Molecular and Biochemical Characterization of a Novel β-N-Acetyl-D-Hexosaminidase with Broad Substrate-Spectrum from the Aisan Corn Borer, Ostrinia Furnacalis

Liu¹,

Liu²,

Qu³

et al. 2012

Int. J. Biol. Sci.

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Insect β-N-acetyl-D-hexosaminidases with broad substrate-spectrum (IBS-Hex) are the homologues of human β-N-acetyl-D-hexosaminidase A/B (HsHex A/ B). These enzymes are distributed in most insect species and vary in physiological roles. In this study, the gene encoding an IBS-Hex, OfHEX2, was cloned from the Asian corn borer, Ostrinia furnacalis. Recombinant OfHex2 was expressed in Pichia pastoris and purified to homogeneity. By structure-based sequence alignment, three sequence segments with high diversity among IBS-Hexs were firstly concluded. Furthermore, the residue pair N423-R424/ D452-L453 important for the specificity of human β-N-acetyl-D-hexosaminidase subunits α/β toward charged/ non-charged substrates was not conserved in OfHex2 and other IBS-Hexs. Unlike HsHex A, OfHex2 could not degrade charged substrates such as 4-methylumbelliferyl-6-sulfo-N-acetyl-β-D-glucosaminide, ganglioside GM2 and peptidoglycan. OfHex2 showed a broad substrate-spectrum by hydrolyzing β1-2 linked N-acetyl-D-glucosamines from both α3 and α6 branches of biantennary N-glycan and β1-4 linked GlcNAc from chitooligosaccharides as well as β1-3 linked or β1-4 linked N-acetyl-D-galactosamine from oligosaccharides of glycolipids. Real-time PCR analysis demonstrated that the expression of OfHEX2 was up-regulated in the intermolt stages (both larva and pupa), and mainly occurred in the carcass rather than in the midgut during the feeding stage of fifth (final) instar larva. This study reported a novel IBS-Hex with specific biochemical properties, suggesting biodiversity of this class of enzymes.

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“…Fucosidases, mannosidases, and two -N-acetylhexosaminidases (named HEXA and HEXB) are present and conserved on the sperm surface of different species across the Drosophila genus (Cattaneo, Ogiso, Hoshi, Perotti, & Pasini, 2002;Cattaneo et al, 2006;Intra et al, 2006Intra et al, , 2011Intra, Cenni, Pavesi, Pasini, & Perotti, 2009). Moreover, the plasma membrane of Ceratitis capitata spermatozoa has an -mannosidase, an -L-fucosidase, and a -N-acetylhexosaminidase too (Intra et al, 2011;Pasini et al, 2010). More recently, the presence of a mannosidase and a -N-acetylglucosaminidase on the sperm surface of the Hemipteran Aquarius remigis has been identified (Stephens, Thaler, & Cardullo, 2015).…”

Section: Introductionmentioning

confidence: 99%

In vitro evidence for the participation of Drosophila melanogaster sperm β‐N‐acetylglucosaminidases in the interactions with glycans carrying terminal N‐acetylglucosamine residues on the egg's envelopes

Intra

Veltri

et al. 2017

Arch Insect Biochem Physiol

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Fertilization is a complex and multiphasic process, consisting of several steps, where egg-coating envelope's glycoproteins and sperm surface receptors play a critical role. Sperm-associated β-N-acetylglucosaminidases, also known as hexosaminidases, have been identified in a variety of organisms. Previously, two isoforms of hexosaminidases, named here DmHEXA and DmHEXB, were found as intrinsic proteins in the sperm plasma membrane of Drosophila melanogaster. In the present work, we carried out different approaches using solid-phase assays in order to analyze the oligosaccharide recognition ability of D. melanogaster sperm hexosaminidases to interact with well-defined carbohydrate chains that might functionally mimic egg glycoconjugates. Our results showed that Drosophila hexosaminidases prefer glycans carrying terminal β-N-acetylglucosamine, but not core β-N-acetylglucosamine residues. The capacity of sperm β-N-acetylhexosaminidases to bind micropylar chorion and vitelline envelope was examined in vitro assays. Binding was completely blocked when β-N-acetylhexosaminidases were preincubated with the glycoproteins ovalbumin and transferrin, and the monosaccharide β-N-acetylglucosamine. Overall, these data support the hypothesis of the potential role of these glycosidases in sperm-egg interactions in Drosophila.

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Identification and expression profiling of Ceratitis capitata genes coding for β-hexosaminidases

Cited by 12 publications

References 61 publications

A Sperm–Plasma β-N-Acetyl-D-Hexosaminidase Interacting with a Chitinolytic β-N-Acetyl-D-Hexosaminidase in Insect Molting Fluid

A Sperm–Plasma β-N-Acetyl-D-Hexosaminidase Interacting with a Chitinolytic β-N-Acetyl-D-Hexosaminidase in Insect Molting Fluid

Molecular and Biochemical Characterization of a Novel β-N-Acetyl-D-Hexosaminidase with Broad Substrate-Spectrum from the Aisan Corn Borer, Ostrinia Furnacalis

In vitro evidence for the participation of Drosophila melanogaster sperm β‐N‐acetylglucosaminidases in the interactions with glycans carrying terminal N‐acetylglucosamine residues on the egg's envelopes

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