3D structure analysis of Ata protein in Acinetobacter baumannii

Acinetobacter baumannii is a strictly aerobic, Gram-negative coccobacillus that is now a major cause of nosocomial infections worldwide, particularly in patients who are critically ill, those requiring mechanical ventilation in the intensive care units (ICUs), and also among injured soldiers returning from the Iraq and Afghanistan conflicts. Many A. baumannii isolates manifest high levels of resistance to antibiotics such as ampicillin-sulbactam, carbapenems, aminoglycosides, tetracyclines, and quinolones. Of particular concern is the emergence of A. baumannii strains resistant to all commonly used antibiotics, including colistin, polymyxin B, or tigecycline. Furthermore, A. baumannii displays an extraordinary tolerance to desiccation and disinfectants, which contributes to its long-term persistence in the hospital environment and the occurrence of outbreaks of infection. PCR analysis of 75 clinical strains of A. baumannii obtained from various geographical locations and types of infections revealed that 44/75 (58.6%) of the strains were positive for ata by PCR, 43 of which (56.3%) produced variable but mostly high levels of surface Ata, as detected by flow cytometry. In the present study we predicted 3D structure of Ata protein in acinetobacter baumannii via in silico approaches and evaluated the functional properties of residues which involved in ligand binding site

کلیدواژه ها:

Acinetobacter baumannii ، ligand binding site ، Bioinformatic