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Article in Chinese | WPRIM | ID: wpr-340617


<p><b>OBJECTIVE</b>To investigate the effects of antibiotic stewardship on the pathogen and clinical outcome of neonatal bloodstream infections (BSIs).</p><p><b>METHODS</b>A retrospective study was performed on neonates with BSIs who were admitted to the neonatal ward in the years of 2010 (pre-stewardship) and 2013 (post-stewardship) for pathogens, antibiotic resistance, antibiotic use, and clinical outcomes.</p><p><b>RESULTS</b>The admission rate of BSIs (6.47% vs 2.78%) and the incidence of nosocomial BSIs (0.70% vs 0.30%) in 2013 were significantly higher than in 2010 (P<0.01). However, there were no signicant differences in the clinical outcomes between the years of 2010 and 2013 (P>0.05). The four most common pathogens isolated from blood cultures, Staphylococcus haemolyticus, Staphylococcus epidermidis, Klebsiella pneumoniae ssp pneumoniae and E.coli, were similar between the two years. There were no significant differences in the detection rates of extended spectrum β-lactamase-positve Klebsiella pneumoniae ssp pneumoniae or E.coli between the two years. The detection rates of methicillin-resistant Staphylococcus/β-lactamase-positive Staphylococcus haemolyticus and Staphylococcus epidermidis were similar between the two years (P>0.05).</p><p><b>CONCLUSIONS</b>Since the implementation of antibiotic stewardship, there has been no marked variation in the common pathogens and their antibacterial resistance in neonatal BSIs. The antibiotic stewardship could promote the recovery of patients with BSIs.</p>

Anti-Bacterial Agents , Therapeutic Uses , Bacteria , Drug Resistance, Microbial , Humans , Infant, Newborn , Neonatal Sepsis , Drug Therapy , Microbiology , Retrospective Studies , Time Factors
Article in Chinese | WPRIM | ID: wpr-353217


<p><b>OBJECTIVE</b>To study the expression and purification of a fusion protein of ricin A chain (RTA) and green fluorescent protein (GFP).</p><p><b>METHODS</b>The DNA sequence encoding ricin A chain was inserted into pEGFPC1 first to make the template sequence of the fusion protein. The fusion gene was amplified from the plasmid pEGFP-RTA by PCR, and directly subcloned into T vector. The fusion gene then was cloned into expression vector pET-28a(+), and the sequence was confirmed by sequencing. Expression was induced by IPTG in E. coli BL21(DE3). The fusion protein was purified by metal chelated affinity chromatography. The cytotoxicity of fusion protein was analyzed by the MTT assay in HepG2 and Hela cells.</p><p><b>RESULTS</b>The fusion protein of ricin A chain and GFP could be produced in E. coli transformed with the expression plasmid of pET-28a(+)-GFP-RTA. The molecular weight of the recombinant protein was measured by SDS-PAGE. The fusion protein showed a green fluorescence and had a similar cytotoxicity of RTA.</p><p><b>CONCLUSION</b>A recombinant fusion protein of RTA and GFP expressed in E. coli is possessed of similar biological activity of individual GFP and RTA, which could be used in study of the intracellular trafficking and translocation of RTA.</p>

Escherichia coli , Genetics , Metabolism , Green Fluorescent Proteins , Genetics , HeLa Cells , Humans , Luminescent Proteins , Genetics , Recombinant Fusion Proteins , Genetics , Ricin , Genetics