Search

Background: Carbapenem-resistant A. baumannii (CRAB) bacterium is difficult to treat with available antimicrobial agents leading to use a few antibiotics such as colistin as an option for treatment. However, the use of the colistin has serious side effects and leads to developing bacterial resistance. Objective: This study aimed to determine effectiveness of phage/colistin combination to inhibit biofilm formation of CRAB. Methods: Sixty clinical A. baummanii isolates were identified with the VITEKII system and 16S rRNA gene. The antibiotic susceptibility and detection of Oxacillinases genes were tested for all isolates. Results: The antibiotic sensitivity of A. baumannii isolates showed a high resistance percentage to Ceftriaxone (CRO) with 92% (55 isolates), and Cefotiam (CTF) with 87% (52 isolates), while the lowest percent related to Colistin (CO) with 17% (10 isolates). The results of antibiotic resistance and Oxacillinases genes reported that only 14 isolates from the current study were CRAB. Phage and host A. baumannii of phage were isolated and characterized previously. Biofilm production assay of CRAB isolates were showed that among 14 isolates including the phage host: 57% (8) was weak and 43% (6) was moderate biofilm producer. Therefore, the synergistic effect of a combination ΦKAB phage in MOI (10) and Colistin with MIC=8 µg/ml against CRAB isolates was evaluated and showed complete transfer of isolates by 100 % to weak biofilm producer compared with CRAB isolates. Conclusions: Among 60 isolates of A. baumannii, most isolates were MDR 44 (73.3%) and only 14 (23.3%) isolates were CRAB that were 57% weak and 43% moderate biofilm producers. The mixture of Colistin/ΦKAB phage could inhibit and reduce biofilm forming in CRAB isolates. Overall, the present study may provide evidence on the capability of the isolated phage to serve as a novel strategy to treat infections caused by MDR A. baumannii. [ABSTRACT FROM AUTHOR]

Copyright of Al-Mustansiriyah Journal of Science is the property of Republic of Iraq Ministry of Higher Education & Scientific Research (MOHESR) and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Al-Mustansiriyah Journal of Science is the property of Republic of Iraq Ministry of Higher Education & Scientific Research (MOHESR) and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

In silico analyses identified a Crp/Fnr family transcription factor (HcpR) in sulfate-reducing bacteria that controls expression of the hcp gene, which encodes the hybrid cluster protein and contributes to nitrosative stress responses. There is only one hcpR gene in the model sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough, but two copies in Desulfovibrio desulfuricans 27774, which can use nitrate as an alternative electron acceptor to sulfate. Structures of the D. desulfuricans hcpR1, hcpR2 and hcp operons are reported. We present evidence that hcp expression is regulated by HcpR2, not by HcpR1, and that these two regulators differ in both their DNA-binding site specificity and their sensory domains. HcpR1 is predicted to be a b-type cytochrome. HcpR1 binds upstream of the hcpR1 operon and its synthesis is regulated coordinately with hcp in response to NO. In contrast, hcpR2 expression was not induced by nitrate, nitrite or NO. HcpR2 is an iron-sulfur protein that reacts with NO and O2. We propose that HcpR1 and HcpR2 use different sensory mechanisms to regulate subsets of genes required for defense against NO-induced nitrosative stress, and that diversification of signal perception and DNA recognition by these two proteins is a product of D. desulfuricans adaptation to its particular environmental niche. [ABSTRACT FROM AUTHOR]

The Escherichia coli Fumarate-Nitrate Reduction regulator (FNR) protein is the paradigm for bacterial O2-sensing transcription factors. However, unlike E. coli, some bacterial species possess multiple FNR proteins that presumably have evolved to fulfill distinct roles. Here, three FNR proteins (ANR, PP_3233 and PP_3287) from a single bacterial species, Pseudomonas putida KT2440, have been analyzed. Under anaerobic conditions, all three proteins had spectral properties resembling those of [4Fe-4S] proteins. The reactivity of the ANR [4Fe-4S] cluster with O2 was similar to that of E. coli FNR and during conversion to the apo-protein, via a [2Fe-2S] intermediate, cluster sulfur was retained. Like ANR, reconstituted PP_3233 and PP_3287 were converted to [2Fe-2S] forms when exposed to O2, but their [4Fe-4S] clusters reacted more slowly. Transcription from an FNR-dependent promoter with a consensus FNR-binding site in P. putida and E. coli strains expressing only one FNR protein was consistent with the in vitro responses to O2. Taken together the experimental results suggest that the local environments of the iron-sulfur clusters in the different P. putida FNR proteins influence their reactivity with O2, such that ANR resembles E. coli FNR and is highly-responsive to low concentrations of O2, whereas PP_3233 and PP_3287 have evolved to be less sensitive to O2. [ABSTRACT FROM AUTHOR]