Biochemical and immunological characterization of excretory-secretory products of Vesicocoelium solenophagum and plasma proteins of its bivalve host, Sinonovacula constricta.
In this study, the excretory-secretory products (ESP) of the daughter sporocysts of Vesicocoelium solenophagum (Trematoda) and plasma proteins of its host, Sinonovacula constricta were characterized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and gelatin-substrate gel analyses, and the relationships between them were analysed using immunoblotting. Proteinase activity was detected in the ESP from daughter sporocysts of V. solenophagum. Some polypeptides of the ESP were found to be recognized by antiserum, raised against plasma from non-infected S. constricta, suggesting that the ESP may mimic host molecules (molecular mimicry). In contrast, neither the obvious proteinase activity nor the binding to the antisera was observed for the soluble proteins of daughter sporocyst, indicating that the ESP may play a important role in the parasite-host relationship. Although the plasma of infected S. constricta contained polypeptides that were similar to the plasma of non-infected bivalves, increased quantities of proteins at >170 kDa, 15 kDa and decreased quantities at 60 kDa were observed in the plasma of infected bivalves. Immunoblotting analysis revealed that the plasma of infected bivalves had a faint reaction with both anti-non-infected plasma antisera and anti-sporocyst antisera. These results indicated that the structure and quantity of some polypeptides from the plasma of infected bivalves had changed because of the infection with V. solenophagum. The polypeptides between the plasma of bivalves from a non-epidemic area and that from an epidemic area were similar, but the former had more polypeptides of 170-220 kDa and much greater proteinase activity than the latter, suggesting that the increased polypeptides of 170-220 kDa and the high proteinase activity in plasma may be favourable for protecting the host from being invaded by the parasites.
Shi
L
L
School of Life Science, Xiamen University, Fujian, People's Republic of China. leishi@jingxian.xmu.edu.cn.
Wang
J
J
D000818:Animals; D001798:Blood Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D015801:Helminth Proteins / Q000032:analysis*; D006790:Host-Parasite Interactions; D015151:Immunoblotting; D018716:Molecular Mimicry; D008970:Molecular Weight; D008974:Mollusca / Q000276:immunology* / Q000469:parasitology; D010274:Parasitology / Q000379:methods; D014200:Trematoda / Q000737:chemistry / Q000378:metabolism*
D001798:Blood Proteins; D015801:Helminth Proteins