Analysis of penicillin-binding proteins (PBPs) in carbapenem resistant Acinetobacter baumannii.

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dc.contributor.authorVashist, Jitendra
dc.contributor.authorTiwari, Vishvanath
dc.contributor.authorDas, Rituparna
dc.contributor.authorKapil, Arti
dc.contributor.authorRajeswari, Moganty R
dc.date.accessioned2011-11-21T10:45:48Z
dc.date.available2011-11-21T10:45:48Z
dc.date.issued2011-03
dc.description.abstractBackground & objectives : Acinetobacter baumannii is a Gram-negative, cocco-bacillus aerobic pathogen responsible for nosocomial infections in hospitals. In the recent past A. baumannii 0had developed resistance against β-lactams, even against carbapenems. Penicillin-binding proteins (PBPs) are crucial for the cell wall biosynthesis during cell proliferation and these are the target for β-lactams. Therefore, the present study was carried out to identify the PBPs in three (low, intermediate and high MICs) groups of carbapenem resistant isolates strains of A. baumannii. Methods: ATCC 19606 and 20 β-lactam resistant isolates of A. baumannii were obtained. Selective identification of the PBPs was done using Bocillin FL, a non-radioactive fluorescent derivative of penicillin. Results: The fluorescence emission from Bocillin-tag in SDS-PAGE gel of native strain identified eight PBPs, with apparent molecular weight of 94, 65, 49, 40, 30, 24, 22 and 17 kDa, however, these PBPs revealed alteration in carbapenem-resistant isolates. Interpretation & conclusions: A comparative analysis of PBPs in the resistant isolates with those of ATCC revealed a decreased expression of all PBPs except that of 65 and 17 kDa PBPs which were marginally downregulated, and simultaneous appearance of new 28 kDa PBP (in low and intermediate resistant isolates) and 36 kDa in high meropenem resistant group of A. baumannii. The present study indicated an association between alteration in PBPs and β-lactam resistance in A. baumannii.en_US
dc.identifier.citationVashist Jitendra, Tiwari Vishvanath, Das Rituparna, Kapil Arti, Rajeswari Moganty R. Analysis of penicillin-binding proteins (PBPs) in carbapenem resistant Acinetobacter baumannii. Indian Journal of Medical Research. 2011 Mar; 133(3): 332-338.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/135394
dc.language.isoenen_US
dc.source.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3103161/en_US
dc.subjectAcinetobacter baumanniien_US
dc.subjectBocillin FLen_US
dc.subjectβ-lactam resistanceen_US
dc.subjectpenicillin-binding proteinsen_US
dc.subject.meshAcinetobacter baumannii --drug effects
dc.subject.meshAcinetobacter baumannii --metabolism
dc.subject.meshAmino Acid Sequence
dc.subject.meshAnti-Bacterial Agents --pharmacology
dc.subject.meshCarbapenems --pharmacology
dc.subject.meshDrug Resistance, Microbial
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshMicrobial Sensitivity Tests
dc.subject.meshMolecular Sequence Data
dc.subject.meshPenicillin-Binding Proteins --chemistry
dc.subject.meshPenicillin-Binding Proteins --metabolism
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
dc.titleAnalysis of penicillin-binding proteins (PBPs) in carbapenem resistant Acinetobacter baumannii.en_US
dc.typeArticleen_US
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