Histopathological alterations in the liver of intermediated hosts infected with Echinococcus granulosus parasite can be occurred by necrotic expansion as a result of an increase in growth of the parasite larva stage (metacestode), which may cause perturbation in production of liver function markers. Thus, this study aims to determinate the liver biochemical profile and some serum electrolytes of E. granulosus-infected sheep at different hydatid cyst infection ratios (IRs). fifty livers from naturally E. granulosusinfected sheep with five livers from uninfected-sheep as a control group were enrolled in this study. Cardiac blood samples under sterilized conditions were gently collected and isolated sera were biochemically assayed for determination of liver function markers including; Aspartate transaminase (AST), Alanine transaminase (ALT), alkaline phosphatase (ALP), Albumin (ALB) and total protein (TP), as well as the level of some serum electrolytes including Ca, K, Na and Cl using fully automatic biochemical analyzer, FUJI-Film. The current data indicated a progressive increase in the level of AST, ALT, ALP, Ca and K. The level of ALB and TP were gradually declined with a rise of liver infection ratio with hydatid cysts. In conclusion, the current findings indicated perturbation of liver function markers and the level of some serum electrolytes, mainly Ca and K in E. granulosus-infected sheep based on the infection ratio of liver. Additionally, acute and chronic infection of E. granulosus parasites in sheep can be determined based on the level of liver function markers in serum.
Echinococcus granulosus is a causative agent of cystic echinococcosis disease which represents a real challenge of health and economic sectors by threatening human and animal life. In E. granulosus-infected intermediate hosts, the local immune responses represent by balance between T helper-1 (Th1)/Th2 responses and involving of IL-10-secreting CD8+ T cells, as well as induction of antigen presentation and production of antibodies were suggested. Spill out of hydatid cyst fluid from ruptured cysts can induce deadly anaphylactic reactions. Although the host promotes effective immune responses against E. granulosus infection, the parasite can be survived, suggesting exist of mechanisms of immune evasion that help E. granulosus to grow and develop. Several mechanisms of immune evasion have been suggested during E. granulosus infection including; antigenic variation that lead to produce useless antibodies, alteration of Th1/Th2 cytokine profile, anti-apoptotic process, molecular mimicry and interfering with Antigen presentation, as well as fibrosis of hydatid cysts can be occurred in chronic cases. Furthermore, as an efficient drug against E. granulosus infection still not available, immunization of hosts could be necessary. Interestingly, combination of multiple EG95 proteins of oncospheres from the different isomers could possibly maximize the EG95 vaccine efficacy.
The study investigated the effect of the lipopolysaccharide, (LPS) extracted from Klebsiella pneumoniae, on immune response of BALB/c mice infected with secondary hydatid disease caused by Echinococcus granulosus protoscoleces.
The study tested the effect of the lipopolysaccharide, which was extracted from Klebsiella pneumoniae, on immune response of BALB/c mice infected with secondary hydatid disease caused by experimental infection with Echinococcus granulosus protoscolices.
Ligases enzymes were discovered as a member of the nucleotidyl transferase family. Here in this paper, DNA Ligase is extracted from S. aureus works with the cofactor NAD + to make a phosphodiester bond and reform between the 3'hydroxyl and 5'phosphate DNA end. Staphylococcus aureus-DNA Ligases Enzyme type A (SLE-A) contains two essential domains; NTase and OB-fold domain, which are the most essential domains for the enzyme function. The main aim of the study is to investigate the activity of SLE-A in the presence of magnesium ion (Mg +2 ) by evaluating several kinetic parameters on a time course. The result showed that SLE-A has optimal activity at 500 µM of Mg +2 . Furthermore, the low number of Equilibrium Association Constant (K m value) explains the binding affinity between DNA ligase of Staphylococcus aureus SLE-A enzyme and Mg +2 ion was very high and sold.
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