Evidence for a family of schistosome glycan-binding lectins in Biomphalaria afexandrina

Molecular and functional characterization of a tandem-repeat galectin from the freshwater snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni

“…In earlier studies galactose-reactive lectins have been identified and isolated from the plasma of various molluscs (Suzuki and Mori, 1989;Mitra and Sakar, 1998), including B. glabrata (Mansour, 1996), but their identities as authentic galectins were not determined. Therefore, the presence/absence of plasma galectins within mollusks has not been fully resolved.…”

“…Thus, there is substantial support for the existence of this 4 gene family in molluscs. However, although galactose-binding proteins previously have been reported in the hemolymph of bivalve (Suzuki andMori, 1989, Baldo et al, 1975), gastropod (Mitra and Sakar, 1998;Mansour, 1996), and cephalopod (Rogener et al, 1985) molluscs, their molecular structures, expression profiles and specific role(s) in the internal defense system of these organisms remain unknown.…”

Distinct binding patterns of fucose-specific lectins from Biomphalaria alexandrina and Lotus tetragonolobus to murine lymphocyte subsets

“…These include the relatively well-characterized Lotus tetragonolobus (Pereira and Kabat, 1974) and Ulex europaeus (Pereira et al, 1978;Baldus et al, 1996) lectins from plants, the Anguilla lectins from eels (Honda et al, 2000;Bianchet et al, 2002) as well as the Aleuria aurantia lectin from mushrooms (Nagata et al, 1991). A novel family of isolectins, that selectively recognize a schistosomeassociated (Fuca1-2) Gala1-2Glc sequence, has been identified as part of the humoral defense mechanisms of Biomphalaria alexandina, the snail vector of Schistosoma mansoni (Mansour, 1995;Mansour et al, 1995). Three lectins of this family, designated BaSI, BaSII and BaSIII, have been structurally characterized as tetramers constituted by the combinatorial association of a diversity of subunits that arise by both genetic and post-translational mechanisms (Mansour, 1995).…”

“…A novel family of isolectins, that selectively recognize a schistosomeassociated (Fuca1-2) Gala1-2Glc sequence, has been identified as part of the humoral defense mechanisms of Biomphalaria alexandina, the snail vector of Schistosoma mansoni (Mansour, 1995;Mansour et al, 1995). Three lectins of this family, designated BaSI, BaSII and BaSIII, have been structurally characterized as tetramers constituted by the combinatorial association of a diversity of subunits that arise by both genetic and post-translational mechanisms (Mansour, 1995). Employing these lectins in epitope localization studies has established the expression of the a1-2 fucosylated epitope in multiple copies among acidic glycoproteins synthesized by adult and larval stages of both S. mansoni Mansour, 1996) and the related trematode Fasciola hepatica (Abdul-Salam and .…”

Biomphalaria glabrata embryonic cells express a protein with a domain homologous to the lectin domain of mammalian selectins

“…Mansour (1995) isolated and characterized a family of isolectins (BaSI, BaSII, BaSIII) from the hemolymph of B. alexandrina, another snail host for S. mansoni, which recognized a fucosyllactose determinant on miracidia . One of these lectins was used to identify glycoproteins bearing the fucosyllactose determinant in adult males and cercariae (Mansour 1996;Negm 1996).…”