الفهرس 
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Abstract
S. aureus is a Gram-positive facultative bacterial pathogen primarily infecting individuals who are hospitalized and suffer from severs underlying diseases. S. aureus can cause a range of infections such as diseases of digestive system, urinary tract infections, diseases of pneumonia, meningitis, osteomyelitis, endocarditis, toxic shock syndrome, bacteremia, and sepsis. This study was conducted to evaluate alpha hemolysin toxin for identification of S. aureus isolates. Also the most active strain producing alpha hemolysin toxin was selected, and alpha hemolysin toxin gene was isolation and cloning. Clinical samples were collected, regardless the type of infection. This study was carried out over a period. 108 samples were collected from different wards in (CMUH). Out of 108 samples, 30 yielded positive culture results for S. aureus. Phenotypic characterization was performed using cultural characteristics and morphological appearance in Gram stained and biochemical identification. Cultivation of S. aureus on blood agar media was used for alpha hemolysin toxin identification. α- toxin was detected 33.33%. SDS-PAGE analyses used to identification and differentiation S. aureus isolates from different infections. In this study, S. aureus isolates can be divided into two different groups according to the presence of the protein patterns which presented or not of alpha hemolysin band (34 KDa). RT-PCR for detection the presence of hia gene in the 11 selected S. aureus isolates was performed. hia genes were detected (90.91 %). from our results, The strain no. 5 had high expression, so the hia gene of strain no. 5 was isolation, sequence and cloning. Our result confirmed the present of hia gene in strain no. 5 which isolated from blood sample. hia gene of strain no. 5 was cloning and expression. Our results confirmed the successful cloning alpha hemolysin by the production of α-toxin protein. The purified alpha hemolysin protein (34 KDa) was detected by SDS-PAGE. Cytotoxicity of recombinant alpha hemolysin protein was detected by using different concentrations for determination the cell viability of four cell lines ( HepG-2, HCT-116, MCF-7, A-549). The cell viability of cell lines were represented 31.69% in HepG-2, 36.27% in HCT-116, 78.95% in MCF-7, 67.28% in A-549. Alpha hemolysin protein had high inhibitory activity against HepG-2 and HCT-116, and had weak inhibitory activity against MCF-7 and A-549. Our results confirmed that the purified α- toxin protein was used as anticancer agent. The obtained results concluded that the production of recombinant α- toxin was very simple process, low cost, high efficiency, non-toxic, high yield and no side effect, and the purified α-toxin protein can used as anticancer durg.