Biomphalaria glabrata embryonic cells express a protein with a domain homologous to the lectin domain of mammalian selectins.
We have cloned from Biomphalaria glabrata, the intermediate host of the helminth parasite Schistosoma mansoni, a 36-kDa apparent-molecular-mass molecule (BgSel) that shares sequence identity with selectins of the cell-adhesion-molecule superfamily. BgSel exhibited in its C-terminal part a putative C-type lectin domain similar to the selectin lectin domain. Using antibodies to the recombinant BgSel protein, we demonstrated the presence of BgSel in snail hemocytes as well as in the cell line derived from B. glabrata embryos (Bge). Anti-BgSel antibodies specifically recognized a 79-kDa component in Bge-cell-secreted products that was supposed to represent the native form of BgSel, as was confirmed after glycosidase treatment. Lectins are known to be implicated in recognition mechanisms participating in humoral and cellular immunity in molluscs. The possible role of BgSel in the interaction between sporocysts and Bge cells, particularly in the in vitro model of sporocyst development dependent on Bge cell factors, remains to be determined.
Duclermortier
P
P
INSERM U167, Institut Pasteur, Lille, France.
Lardans
V
V
Serra
E
E
Trottein
F
F
Dissous
C
C
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001700:Biomphalaria / Q000196:embryology* / Q000235:genetics*; D003001:Cloning, Molecular; D017124:Conserved Sequence; D037102:Lectins / Q000096:biosynthesis / Q000235:genetics*; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis; D019087:Selectins / Q000096:biosynthesis / Q000235:genetics*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D037102:Lectins; D012333:RNA, Messenger; D011994:Recombinant Proteins; D019087:Selectins; C120002:selectin 1, Biomphalaria glabrata