RESUMO
Cockroaches are very capable of mechanically transmitting harmful microorganisms, which is seen to be a severe hazard to the general public's health. The purpose of this study was the evaluation of cockroach bacterial contamination in various locations throughout Babylon. 300 cockroaches were caught from different wards of the hospital, restaurants, and houses. Using PBS buffer, the external surface of the cockroaches was washed to collect bacteria. Standard phenotypic methods were used to identify and classify bacteria. Afterward, the bacterial resistance to different antibiotics was investigated using the Kirby-Bauer disk diffusion susceptibility test. The 200 (66.6 %) American cockroaches including 56 (18.7 %) Blattella germanica and 44 (14.6 %) Blatta orientalis were identified. Noteworthy, 96.6 % of cockroaches were infected with different bacteria. Bacillus strains, coagulase-negative Staphylococci (CoNs), and Escherichia coli were the most frequent among the isolated bacteria. On average, the highest antibiotic resistance was detected to cefotaxime, ampicillin, cephalothin, and kanamycin. On the other hand, the isolated bacteria showed high sensitivity to gentamicin, nitrofurantoin, tetracycline, trimethoprim/sulfamethoxazole (SXT), and chloramphenicol. high antibiotic resistance in bacteria isolated from different wards of the hospital and the high potential of transmission of these bacteria by cockroaches is a serious warning for the health of society.
RESUMO
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzyme defect that affects more than 500 million people worldwide. Individuals affected with G6PD deficiency may occasionally suffer mild-to-severe chronic hemolytic anemia. Chronic non-spherocytic hemolytic anemia (CNSHA) is a potential result of the Class I G6PD variants. This comparative computational study attempted to correct the defect in variants structure by docking the AG1 molecule to selected Class I G6PD variants [G6PDNashville (Arg393His), G6PDAlhambra (Val394Leu), and G6PDDurham (Lys238Arg)] at the dimer interface and structural NADP+ binding site. It was followed by an analysis of the enzyme conformations before and after binding to the AG1 molecule using the molecular dynamics simulation (MDS) approach, while the severity of CNSHA was determined via root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), hydrogen bonds, salt bridges, radius of gyration (Rg), solvent accessible surface area analysis (SASA), and principal component analysis (PCA). The results revealed that G6PDNashville (Arg393His) and G6PDDurham (Lys238Arg) had lost the direct contact with structural NADP+ and salt bridges at Glu419 - Arg427 and Glu206 - Lys407 were disrupted in all selected variants. Furthermore, the AG1 molecule re-stabilized the enzyme structure by restoring the missing interactions. Bioinformatics approaches were also used to conduct a detailed structural analysis of the G6PD enzyme at a molecular level to understand the implications of these variants toward enzyme function. Our findings suggest that despite the lack of treatment for G6PDD to date, AG1 remains a novel molecule that promotes activation in a variety of G6PD variants.
