Functional characterization of phospholipase B enzyme from Giardia lamblia

被引:2
作者
Sarkar, Rituparna [1 ]
Sardar, Sanjib Kumar [1 ]
Ghosal, Ajanta [1 ]
Das, Koushik [1 ,2 ]
Saito-Nakano, Yumiko [3 ]
Dutta, Shanta [4 ]
Nozaki, Tomoyoshi [5 ]
Ganguly, Sandipan [1 ]
机构
[1] ICMR Natl Inst Cholera & Enter Dis, Div Parasitol, Kolkata, India
[2] Univ Petr & Energy Studies, Sch Hlth Sci & Technol, Dept Allied Hlth Sci, Dehra Dun, India
[3] Natl Inst Infect Dis NIID, Dept Parasitol, Tokyo, Japan
[4] ICMR Natl Inst Cholera & Enter Dis ICMR NICED, Div Bacteriol, Kolkata, India
[5] Univ Tokyo, Sch Int Hlth, Grad Sch Med, Dept Biomed Chem, Tokyo, Japan
关键词
Phospholipase B; Giardia lamblia; Phospholipase; Oxidative stress; OXIDATIVE STRESS; PURIFICATION; CRYPTOSPORIDIUM; A(2); CELL; INHIBITION; ACID; GENE;
D O I
10.1016/j.exppara.2023.108602
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
The microaerotolarent amitochondriate protozoan Giardia lamblia causes Giardiasis and produces a unique enzyme called Phospholipase B (PLB) in contrast to higher eukaryotes. The enzyme is produced upon induction with oxidative (H2O2) stress, thus leading to prostaglandin E2 (PGE2) production. It exists in dimeric form, and its molecular weight is 56 kDa. This PLB was extracellularly cloned in the pET21d vector. The ORF is 1620 bp (Genbank accession no. -OM939681) long and codes for a protein 539 amino acid long, with a 15 amino acid long amino-terminal signal peptide. The highest enzyme activity of PLB was identified at pH 7.5 and 35 degrees C. This specific enzyme was also active at 50 degrees C pH 10, but activity was low. We also analyzed the expression of PLB protein in G. lamblia, which was significantly induced under increased oxidative stress.
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页数:8
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