Expression study of an α-l-fucosidase gene in the Drosophilidae family

Fucosidases of Sperm and Milt in Darters (Percidae: Etheostomatini)

“…Sperm associated -L-fucosidases have been reported in several other organisms and are considered to be strong candidates for important roles during fertilization [11,12,16,[18][19][20][21][22]. This report describes a sperm associated -Lfucosidase in darters, suggesting that fish too may require -L-fucosidase for fertilization.…”

“…Substantial evidence in the literature supports roles for carbohydrates during fertilization [1][2][3][4][5][6][7][8][9][10]. Research over the past two decades has led to the identification of sperm associated -L-fucosidases in humans [11][12][13][14][15] rats [16][17][18], Drosophila [19][20][21], ascidians [22], Unio elongatulus [23], chimpanzees [24], bulls [25] and Syrian hamsters (Venditti, Swann, and Bean, in revision), but not yet in fishes. Additionally, L-fucose has been shown to be important during fertilization [26][27][28][29][30].…”

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

“…DmHEXA and DmHEXB are involved in the primary sperm-egg interactions in D. melanogaster and in other Drosophila species (Perotti et al, 2001;Cattaneo et al, 2006;Intra et al, 2009). A function of α-L-fucosidase as egg receptor in gamete interactions has been hypothesized (Intra et al, 2006(Intra et al, , 2009Pasini et al, 2008), whereas the role of α-mannosidase has not yet been established (Cattaneo et al, 2002). Three D. melanogaster genes, Hexo1, Hexo2 and fdl, codes for the β 1 , β 2 and α subunits which associate to form the heterodimeric DmHEXA, with an αβ 2 structure, and DmHEXB, with a β 1 β 2 structure, present in the sperm plasma membrane (Cattaneo et al, 2006).…”

Drosophila sperm surface alpha-l-fucosidase interacts with the egg coats through its core fucose residues

“…However, in these dipteran species detailed biochemical studies on the complementary ligands of the egg coat and on the oligosaccharide recognition ability of sperm glycosidases are missing. In this study, we have focused our attention on the a-L-fucosidase present on the sperm surface of D. melanogaster and D. ananassae (Intra et al, , 2009Pasini et al, 2008;Xu et al, 2011). Substantial evidence in the literature points toward the importance of L-fucose in many physiological roles, such as immune response (Delves, 1998), signal transduction (Moloney et al, 2000), embryogenesis and development (Solter and Knowles, 1978;Haltwinger and Lowe, 2004), apoptosis (Russell et al, 1998), adhesion of pathogens (Hooper and Gordon, 2001), extravasation of leukocytes (Lowe, 2002), and pathological processes, such as atherosclerosis and cancer (Becker and Lowe, 2003).…”

“…We have previously characterized the Drosophila melanogaster gene coding for an a-L-fucosidase, CG6128 Pasini et al, 2008), and analysis of gene expression revealed that, although it is not testis-specific, this gene is preferentially expressed in the male germ-line (Pasini et al, 2008). Moreover, in in vitro binding assays the fusion protein eGFP-DmFuca, expressed in Trichoplusia ni cell, interacts with fucose residues present on the micropyle of the Drosophila eggshell (Xu et al, 2011).…”