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- 저자 : Quan-Ming Zou (검색결과 4 건)
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Xing Chun Wang,Xiao Yi Bi,Pei Shi Sun,Jin Quan Chen,Ping Zou,Xiao Ming Ma,Jing Zhang,Hai Yu Wang,Xiao Yi Xu 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.5
This study uses microbial methods to research the influence of oxygen (O2) content on the removal efficiency of sulfur dioxide (SO2) and nitrogen oxides (NOx) in a tandem twin-towers desulfurization and denitrification process system. Oxygen can play a significant role in biotrickling towers. Other important factors had already been optimized prior to the study, including inlet concentration, gas flow rate, and temperature. SO2 and NOx were prepared by a chemical method. A gas flow meter was used to regulate nitrogen (N2) that had been stored in steel cylinders. In this way, the O2 content was adjusted in the biotrickling towers by controlling the N2 flow rate. Five gradients of O2 content were selected for investigation, namely 4, 8, 12, 16, and 20%. Results indicated that the SO2 removal efficiency from mixed gas (SO2 and NOx) can reach 100%, from all of the five O2 gradients, in biotrickling towers. In a tandem twin-towers desulfurization and denitrification process system, the NOx removal efficiency and the inlet concentration of nitrogen dioxide (NO2) gradually increased as the O2 content increased. Specifically, the average removal efficiency of NOx increased from 49.28 to 80.85% as the O2 content changed from 4 to 20%. The oxygen levels influenced the removal of NOx but the SO2 removal efficiency in mixed gas was always stable.
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Yan Cheng,Youjun Feng,Ping Luo,Jiang Gu,Shu Yu,Wei-jun Zhang,Yan-qing Liu,Qing-xu Wang,Quan-ming Zou,Xu-hu Mao 한국미생물학회 2009 The journal of microbiology Vol.47 No.4
Shiga toxin 2 (Stx2) is a major virulence factor for enterohemorrhagic Escherichia coli (EHEC), which is encoded by λ lysogenic phage integrated into EHEC chromosome. Stx2A1, A1 subunit of Stx2 toxin has gathered extensive concerns due to its potential of being developed into a vaccine candidate. However, the substantial progress is hampered in part for the lack of a suitable in vitro expression system. Here we report use of the prokaryotic system pET-28a::espA-Stx2A1/BL21 to carry out the fusion expression of Stx2A1 which is linked to E. coli secreted protein A (EspA) at its N-terminus. Under the IPTG induction, EspA- Stx2A1 fusion protein in the form of inclusion body was obtained successfully, whose expression level can reach about 40% of total bacterial protein at 25°C, much higher than that at 37°C. Western blot test suggested the refolded fusion protein is of excellent immuno-reactivity with both monoclonal antibodies, which are specific to EspA and Stx2A1, respectively. Anti-sera from Balb/c mice immunized with the EspA-Stx2A1 fusion protein were found to exhibit strong neutralization activity and protection capability in vitro and in vivo. These data have provided a novel feasible method to produce Stx2A1 in large scale in vitro, which is implicated for the development of multivalent subunit vaccines candidate against EHEC O157:H7 infections.
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( Ding Hong Lei ),( Hao Zeng ),( Lin Ping Huang ),( Yan Dong Dong ),( Yi Jun Duan ),( Xu Hu Mao ),( Gang Guo ),( Quan Ming Zou ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.10
Most of the Helicobacter pylori strains containing the cag pathogenicity island (PAI) have been associated with more severe gastric disease in infected humans. The cag PAI is composed of 27 proteins, and some of the components are required for CagA translocation into host cells as well as induction of proinflammatory cytokines, such as interleukin-8 (IL-8); however, the exact function of most of the components remains unknown or poorly characterized. In this study, we demonstrated that CagT (HP0532), which is an essential structural component of the cag PAI apparatus, plays an important role in the translocation of CagA into host epithelial cells. In addition to being located on the bacterial surface, CagT is also partially localized in the inner membrane, where it acts as a chaperone-like protein and promotes CagA translocation. However, CagT secretion was not detected by immunoprecipitation analysis of cell culture supernatants. Meanwhile, CagT was related to the introduction of IL-8 of the host cell. These results suggest that CagT is expressed on both the inner and outer bacterial membranes, where it serves as a unique type IV secretion system component that is involved in CagA secretion and cag PAI apparatus assembly.
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Li Wang,Xiao-Fei Liu,Shi Yun,Xiao-Peng Yuan,Xu-Hu Mao,Chao Wu,Wei-Jun Zhang,Kai-Yun Liu,Gang Guo,Dong-Shui Lu,Wen-De Tong,Ai-Dong Wen,Quan-Ming Zou 한국미생물학회 2010 The journal of microbiology Vol.48 No.2
A multivalent fusion vaccine is a promising option for protection against Helicobacter pylori infection. In this study, UreB414 was identified as an antigenic fragment of urease B subunit (UreB) and it induced an antibody inhibiting urease activity. Immunization with UreB414 partially protected mice from H. pylori infection. Furthermore, a trivalent fusion vaccine was constructed by genetically linking heat shock protein A (HspA), H. pylori adhesin A (HpaA), and UreB414, resulting in recombinant HspA-HpaA-UreB414 (rHHU). Its protective effect against H. pylori infection was tested in BALB/c mice. Oral administration of rHHU significantly protected mice from H. pylori infection, which was associated with H. pylori-specific antibody production and Th1/Th2-type immune responses. The results show that a trivalent fusion vaccine efficiently combats H. pylori infection, and that an antigenic fragment of the protein can be used instead of the whole protein to construct a multivalent vaccine.
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