DETECTION OF TORQUE TENO VIRUS ANTIGEN AND ASSOCIATED RISK FACTORS AMONG HEMODIALYSIS PATIENTS.

OBJECTIVE: The aim: To determine the prevalence of TTV in patients undergoing hemodialysis and to evaluate the possible risk factors. PATIENTS AND METHODS: Materials and methods: This study was conducted in 93 patients, attending hemodialysis unit at AL-Imammain AL-Kadhimain Medical City Hospital for a period from November 2020 to March 2021. The demographic and clinical characteristics including age, sex, underling medical condition, hepatitis B and C status and laboratory tests such as alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline Phosphatase (ALP) and total serum bilirubin (TSB) were obtained from the record of the patients in hemodialysis unit in the hospital. Direct detection of TTV-Ag was done by enzyme linked immunosorbent assay (ELISA). RESULTS: Results: TTV-Ag was detected in 38 out of 93 (40.9%) hemodialysis patients. Demographic, clinical and risk factors i.e. sex, age, history of diabetes, history of hypertension, history of blood transfusion, number of blood transfusion, the hemodialysis duration, history of surgery and liver enzymes levels did not show significant relation (P>0.05). CONCLUSION: Conclusions: This study showed high prevalence of Torque Teno virus in hemodialysis patients, however, TTV did not play a role in liver injury among these patients.

Molecular cloning, structural modeling and production of recombinant Aspergillus terreusl. asparaginase in Escherichia coli.

l-Asparaginase (EC 3.5.1.1) is an important medical enzyme that catalysis the hydrolysis of l-asparagine to aspartic acid and ammonium. For over four decades l. asparaginase utic agent for the treatment of a variety of lymphoproliferative disorders and lymphoma such as acute lymphoblastic leukemia. In the present study A. terreus full length l. asparaginase gene, 1179bp was optimized for expression in Escherichia coli BL21 (DE3) pLysS. The full length A. terreusl. asparaginase gene encoding a protein of 376 amino acids with estimated molecular weight of 42.0kDa and a theoretical isoelectric point (pI) of 5.0. BLAST and phylogeny analysis revealed that the A. terreusl. asparaginase shared high similarity with other known fungal l. asparaginase (75% homology with A. nomius and 71% with A. nidulans). The recombinant protein was overexpressed in the form of amorphous submicron proteinaceous inclusion bodies upon induction with 1mM IPTG at 37°C for 18h.