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1.
Am J Health Syst Pharm ; 66(12): 1125-31, 2009 Jun 15.
Article in English | MEDLINE | ID: mdl-19498130

ABSTRACT

PURPOSE: The implementation of a quality-monitoring program that identifies and corrects problems associated with using a bar-code-assisted medication administration (BCMA) system is described. SUMMARY: In November 2004, the Bar Code Resource Office assembled a work group to develop a quality program to improve machine-readable, bar-coded medications. The project scope involved the development of a pharmacy-based quality program for unit-dose packaging and bar-code labeling to improve the scanning success rate of bar-coded medications at the point-of-care. Data were collected from facility-based BCMA coordinators at each medical center regarding specific reasons for bedside scanning circumvention, as well as successful scan rates in the pharmacy and at the bedside. The pharmacy and bedside scanning data were aggregated and the baseline of successful scans was determined to be 95%. The reported reasons for scanning circumvention were grouped into six categories: bar-code labeling, missing doses, labels not scanning, error messages, mispackaged medications, and mislabeled medications. The work group developed strategies to mitigate problems in each of the areas. As a result of this effort, the Department of Veterans Affairs created a directive that outlined the best practices for unit-dose packaging and labeling, as well as requirements for ongoing data collection and reporting. CONCLUSION: A quality-monitoring program that identified and provided best-practice recommendations corrected problems associated with using a BCMA system and improved bar-code labeling processes.


Subject(s)
Electronic Data Processing/standards , Medication Errors/prevention & control , Medication Systems, Hospital/standards , Program Development/methods , Humans , Quality Control , United States , United States Department of Veterans Affairs/standards
3.
Mol Microbiol ; 56(1): 68-80, 2005 Apr.
Article in English | MEDLINE | ID: mdl-15773979

ABSTRACT

Sinorhizobium meliloti, a legume symbiont and Brucella abortus, a phylogenetically related mammalian pathogen, both require their BacA proteins to establish chronic intracellular infections in their respective hosts. The lipid A molecules of S. meliloti and B. abortus are unusually modified with a very-long-chain fatty acid (VLCFA; C > or = 28) and we discovered that BacA is involved in this unusual modification. This observation raised the possibility that the unusual lipid A modification could be crucial for the chronic infection of both S. meliloti and B. abortus. We investigated this by constructing and characterizing S. meliloti mutants in the lpxXL and acpXL genes, which encode an acyl transferase and acyl carrier protein directly involved in the biosynthesis of VLCFA-modified lipid A. Our analysis revealed that the unusually modified lipid A is important, but not crucial, for S. meliloti chronic infection and that BacA must have an additional function, which in combination with its observed effect on the lipid A in the free-living form of S. meliloti, is essential for the chronic infection. Additionally, we discovered that in the absence of VLCFAs, S. meliloti produces novel pentaacylated lipid A species, modified with unhydroxylated fatty acids, which are important for stress resistance.


Subject(s)
Acyl Carrier Protein/metabolism , Acyltransferases/metabolism , Heat-Shock Response , Lipid A/metabolism , Medicago sativa/microbiology , Sinorhizobium meliloti/physiology , Symbiosis , Acyl Carrier Protein/genetics , Acyltransferases/genetics , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Fatty Acids/metabolism , Lipid A/chemistry , Sinorhizobium meliloti/enzymology , Sinorhizobium meliloti/genetics , Sinorhizobium meliloti/growth & development
4.
Proc Natl Acad Sci U S A ; 101(14): 5012-7, 2004 Apr 06.
Article in English | MEDLINE | ID: mdl-15044696

ABSTRACT

Sinorhizobium meliloti, a legume symbiont, and Brucella abortus, a phylogenetically related mammalian pathogen, both require the bacterial-encoded BacA protein to establish chronic intracellular infections in their respective hosts. We found that the bacterial BacA proteins share sequence similarity with a family of eukaryotic peroxisomal-membrane proteins, including the human adrenoleukodystrophy protein, required for the efficient transport of very-long-chain fatty acids out of the cytoplasm. This insight, along with the increased sensitivity of BacA-deficient mutants to detergents and cell envelope-disrupting agents, led us to discover that BacA affects the very-long-chain fatty acid (27-OHC28:0 and 29-OHC30:0) content of both Sinorhizobium and Brucella lipid A. We discuss models for how BacA function affects the lipid-A fatty-acid content and why this activity could be important for the establishment of chronic intracellular infections.


Subject(s)
Bacterial Proteins/metabolism , Brucella/metabolism , Fatty Acids/metabolism , Lipid A/metabolism , Membrane Proteins/metabolism , Membrane Transport Proteins/metabolism , Peroxisomes/metabolism , Sinorhizobium/metabolism , Amino Acid Sequence , Bacterial Proteins/chemistry , Gas Chromatography-Mass Spectrometry , Membrane Transport Proteins/chemistry , Molecular Sequence Data , Sequence Homology, Amino Acid , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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