Homology Modeling of Coagulase in Staphylococcus aureus
نویسندگان
چکیده
The close correlation between the ability of coagulase to clot blood plasma and their capacity to produce disease, and the corresponding absence of this property in nonpathogenic strains, have led to the assumption that the coagulase, plays important role in the pathogenesis of disease. Currently, crystal structure of coagulase in Staphylococcus aureus remains indefinable. Thus, the objectives of this research is to generate the three dimensional model of coagulase in S. aureus by using homology modeling approach. In this study, we used bioinformatics tools and databases such as BLAST (Basic Local Alignment Search Tool), GenBank, PDB (Protein Databank), and Discovery Studio to gain specific functional insights into coagulase. The model was validated using protein structure checking tools such as PROCHECK, Verify 3D and CE (Combinatorial Extension) for reliability. Therefore, structure prediction of coagulase in S. aureus can provide preliminary knowledge for understanding the function of the protein. The information from this finding will provide important information into the action and regulation mechanism of the coagulase protein in S. aureus.
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Ciprofloxacin resistance in coagulase-positive and -negative staphylococci: role of mutations at serine 84 in the DNA gyrase A protein of Staphylococcus aureus and Staphylococcus epidermidis.
gyrA mutations in quinolone-resistant pathogenic isolates of Staphylococcus spp. have been detected by the direct HinfI digestion of polymerase chain reaction products. Homology among gyrA genes allowed rapid examination of both coagulase-positive and -negative isolates. DNA sequence analysis revealed that ciprofloxacin resistance in Staphylococcus epidermidis is associated with a novel Ser-84-...
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