Preliminary Investigation into Expression and characterization of Acetylcholinesterase from Bulinus globosus as a potential target for control of Schistosomiasis

Abstract

Bulinus globosus, a freshwater snail, serves as the intermediate host for schistosomiasis, a disease that affects millions globally. Vector control remains a key strategy for disease elimination, and the emergence of resistance highlights the urgent need for novel molluscicides. AChE is a crucial enzyme that could be exploited as a target for controlling this vector.

In this study, AChE was extracted from the hepatopancreas, visceral mass, and foot muscle of B. globosus using established protocols. Partial purification was achieved through ion exchange chromatography using CM-Sephadex C-50 followed by DEAE-Sephadex A-25 chromatography. Kinetic parameters and physicochemical properties of the partially purified enzyme were determined.

Among the tissues analyzed, the hepatopancreas exhibited the highest specific AChE activity (0.591 ± 0.0134 units/mg protein), followed by the foot muscle (0.199 ± 0.0143 units/mg protein) and visceral mass (0.1908 ± 0.0113 units/mg protein). AChE purification folds were 6, 4, and 3 for the hepatopancreas, foot muscle, and visceral mass, respectively. The optimal pH for AChE activity was 8.0 for both the hepatopancreas and visceral mass, and 7.0 for the foot muscle. The Michaelis-Menten constant (K_m) and maximum velocity (V_max) values for AChE were 0.72 mM ± 0.13 and 0.32 ± 0.003 units/mg protein (hepatopancreas), 0.18 mM ± 0.01 and 0.20 ± 0.01 units/mg protein (foot muscle), and 0.18 mM ± 0.014 and 0.20 ± 0.005 units/mg protein (visceral mass).

The differential expression and physicochemical properties of AChE in various tissues of B. globosus suggest its potential as a target for molluscicidal intervention.