Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis

Xuedong He; Jing Zhang; Yue Sun; Tianyan Lan; Xiaola Guo; Xiaoqiang Wang; Omnia M Kandil; Mazhar Ayaz; Xuenong Luo; Houhui Song; Yadong Zheng

doi:10.3390/vetsci9010004

Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis

Vet Sci. 2021 Dec 23;9(1):4. doi: 10.3390/vetsci9010004.

Authors

Xuedong He¹, Jing Zhang², Yue Sun^{3

4}, Tianyan Lan³, Xiaola Guo³, Xiaoqiang Wang⁴, Omnia M Kandil⁵, Mazhar Ayaz⁶, Xuenong Luo³, Houhui Song¹, Yadong Zheng¹

Affiliations

¹ Key Laboratory of Applied Technology on Green-Eco Healthy Animal Husbandry of Zhejiang Province, Zhejiang Provincial Engineering Laboratory for Animal Health Inspection and Internet Technology, College of Animal Science and Technology and College of Veterinary Medicine, Zhejiang A&F University, Hangzhou 311300, China.
² National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention, Key Laboratory of Parasite and Vector Biology, Ministry of Health, National Center for International Research on Tropical Diseases, WHO Collaborating Center for Tropical Diseases, Shanghai 200025, China.
³ State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu Province, Lanzhou Veterinary Research Institute, CAAS, Lanzhou 730046, China.
⁴ School of Chemical and Biological Engineering, Lanzhou Jiaotong University, Lanzhou 730070, China.
⁵ National Research Centre, Departement of Parasitology and Animal Disease, Veterinary Research Division, Giza 12622, Egypt.
⁶ Department of Parasitology, Cholistan University of Veterinary and Animal Sciences, Bahawalpur 73000, Pakistan.

Abstract

Glycolysis is one of the important ways by which Echinococcus multilocularis acquires energy. Fructose-1, 6-bisphosphate aldolase (FBA) plays an important role in this process, but it is not fully characterized in E. multilocularis yet. The results of genome-wide analysis showed that the Echinococcus species contained four fba genes (FBA1-4), all of which had the domain of FBA I and multiple conserved active sites. EmFBA1 was mainly located in the germinal layer and the posterior of the protoscolex. The enzyme activity of EmFBA1 was 67.42 U/mg with K_m and V_max of 1.75 mM and 0.5 mmol/min, respectively. EmFBA1 was only susceptible to Fe³⁺ but not to the other four ions (Na⁺, Ca²⁺, K⁺, Mg²⁺), and its enzyme activity was remarkably lost in the presence of 0.5 mM Fe³⁺. The current study reveals the biochemical characters of EmFBA1 and is informative for further investigation of its role in the glycolysis in E. multilocularis.

Keywords: Echinococcus multilocularis; circular dichroism; enzyme kinetics; fructose-1,6-bisphosphate aldolase 1; secondary structure.