Antibiotics profile and b-lactamases in Pseudomonas aeruginosa | ||||
| Records of Pharmaceutical and Biomedical Sciences | ||||
| Article 8, Volume 5, Pharmacognosy-Microbiology - Serial Number 2, January 2021, Page 74-79 PDF (646.87 K) | ||||
| Document Type: Mini-reviews | ||||
| DOI: 10.21608/rpbs.2021.66592.1095 | ||||
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| Author | ||||
Dalia Mohsen Hamed 
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| Department of Quality control, VACSERA, Giza, Egypt, | ||||
| Abstract | ||||
| Pseudomonas aeruginosa most strains are motile by means of a single polar flagellum. It usually lives in moist environments and uses a wide range of organic compounds for growth, this giving it an exceptional ability to penetrate plant and animal tissues. P.aeruginosa colonizes human body sites, mainly the moist areas, such as the ear, nasal mucosa and throat, as well as stools. It contains 163 known or predicted porin proteins based on its genome sequence, 64 are found as part of 3 families of porins, the OprD-specific porin family, the TonB-dependent gated porin family and the OprM efflux family. β-lactamases are normally located in the periplasm, but it has been detected during the antipseudomonal treatment in the sputum, these enzymes are highly released from high level producers in the lungs. MBL are characterized with zinc ion as a cofactor and with a separate heritage, the common feature of MBLs is the principal zinc binding Histidine-Xhistidine-XAspartic acid in the active site, which coordinates the arrangement of two H2O molecules that are important in the hydrolysis. The chelation of zinc by EDTA or mercaptopropionic acid, impairs β-lactam hydrolysis and restores susceptibility to Carbapenems. MBLs have a wide active site, which let all β-lactams to accomodate in there, except Aztreonam. β-lactamase inhibitors such as clavulanic acid, Tazobactam and Sulbactam are also hydrolised by MBLs. This review was done to figure out the antimicrobial profile and the different β-lactamases present in Pseudomonas aerugionosa | ||||
| Keywords | ||||
| Pseudomonas aeruginosa; metalloβ-lactamases; Carbapenems | ||||
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