Particulate air pollution and respiratory Haemophilus influenzae infection in Mianyang, southwest China.

Particulate air pollution is correlated with many respiratory diseases. However, few studies have focused on the relationship between air particulate exposure and respiratory Heamophilus influenzae infection. Therefore, we detected respiratory Heamophilus influenzae infection by bacterial culture of sputum of patients, and we collected particulate air pollution data (including PM2.5 and PM10) from a national real-time urban air quality platform to analyze the relationship between particulate air pollution and respiratory Heamophilus influenzae infection. The mean concentrations of PM2.5 and PM10 were 37.58 µg/m3 and 58.44 µg/m3, respectively, showing particulate air pollution remains a severe issue in Mianyang. A total of 828 strains of Heamophilus influenzae were detected in sputum by bacterial culture. Multiple correspondence analysis suggested the heaviest particulate air pollution and the highest Heamophilus influenzae infection rates were all in winter, while the lowest particulate air pollution and the lowest Heamophilus influenzae infection rates were all in summer. In a single-pollutant model, each elevation of 10 µg/m3 of PM2.5, PM10, and PM2.5/10 (combined exposure level) increased the risk of respiratory Heamophilus influenzae infection by 34%, 23%, and 29%, respectively. Additionally, in the multiple-pollutant model, only PM2.5 was significantly associated with respiratory Heamophilus influenzae infection (B, 0.46; 95% confidence interval, 0.05-0.87), showing PM2.5 is an independent risk factor for respiratory Heamophilus influenzae infection. In summary, this study highlights air particulate exposure could increase the risk of respiratory Heamophilus influenzae infection, implying that stronger measures need to be taken to protect against respiratory infection induced by particulate air pollution.

Soluble expression, purification, and characterization of active recombinant human tissue plasminogen activator by auto-induction in E. coli.

BACKGROUND: Human tissue plasminogen activator (tPA) belongs to the serine protease family. It converts plasminogen into plasmin and is used clinically to treat thrombosis. Human tPA is composed of 527 amino acids residues and contains 17 disulfide bonds. Escherichia coli has been used only rarely for the efficient production of recombinant tPA. However, the functional expression of full-length tPA that contains multiple disulfide bonds on an industrial scale remains challenging. Here, we describe the soluble expression and characterization of full-length tPA by auto-induction in E. coli. RESULTS: We achieved optimal levels of gene expression, minimized negative effects related to the production of heterologous proteins, and optimized cytoplasmic yields. Three different E. coli strains, BL21 (DE3), Rosetta, and Origami 2, could express tPA using an auto-induction mechanism. In addition, similar yields of recombinant protein were produced at temperatures of 33, 35, and 37°C. The E. coli strain origami 2 could increase disulfide bond formation in cytoplasmic tPA and produce purified soluble recombinant protein (~0.9 mg/l medium). The full-length tPA was monomeric in solution, and fibrin plate assays confirmed that the recombinant tPA displayed serine protease activity. CONCLUSIONS: This is the first report that describes the heterologous expression of correctly folded active full-length tPA. This could provide valuable information for using prokaryotic auto-induction expression systems to produce tPA at industrial and pharmaceutical levels without in vitro refolding during the production step.