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Expression of phenylalanine ammonia lyase as an intracellularly free and extracellularly cell surface-immobilized enzyme on a gut microbe as a live biotherapeutic for phenylketonuria

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Science China(Life Sciences) 2023年第1期66卷 127-136页

作者： Yu Jiang Bingbing Sun Fenghui Qian Feng Dong Chongmao Xu Wuling Zhong Rui Huang Qiwei Zhai Yu Jiang Sheng Yang Shanghai Taoyusheng Biotechology Co. Ltd.Shanghai 201201China CAS Key Laboratory of Synthetic Biology CAS Center for Excellence in Molecular Plant SciencesChinese Academy of SciencesShanghai 200032China Shanghai Research and Development Center of Industrial Biotechnology Shanghai 201201China CAS Key Laboratory of Nutrition Metabolism and Food SafetyShanghai Institute of Nutrition and HealthChinese Academy of SciencesShanghai 200031China

Phenylketonuria(PKU),a disease resulting in the disability to degrade phenylalanine(Phe)is an inborn error with a 1 in 10,000 morbidity rate on average around the world which leads to *** an potential alternative to a protein-restricted diet,oral intake of engineered probiotics degrading Phe inside the body is a promising treatment,currently at clinical stage II(Isabella,et al.,2018).However,limited transmembrane transport of Phe is a bottleneck to further improvement of the probiotic’s ***,we achieved simultaneous degradation of Phe both intracellularly and extracellularly by expressing genes encoding the Phe-metabolizing enzyme phenylalanine ammonia lyase(PAL)as an intracellularly free and a cell surface-immobilized enzyme in Escherichia coli Nissle 1917(EcN)which overcomes the transportation *** metabolic engineering strategy was also combined with strengthening of Phe transportation,transportation of PAL-catalyzed trans-cinnamic acid and fixation of released *** of our final synthetic strain TYS8500 with PAL both displayed on the cell surface and expressed inside the cell to the Pah^(F263S)PKU mouse model reduced blood Phe concentration by 44.4%compared to the control Ec N,independent of dietary protein ***8500 shows great potential in future applications for PKU therapy.

关键词： phenylalanine ammonia lyase cell surface display phenylketonuria TYS8500 oral administration

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surface display of carbonic anhydrase on Escherichia coli for CO_(2) capture and mineralization

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Synthetic and Systems Biotechnology 2022年第1期7卷 460-473页

作者： Yinzhuang Zhu Yaru Liu Mingmei Ai Xiaoqiang Jia Department of Biochemical Engineering School of Chemical Engineering and TechnologyTianjin UniversityTianjin300072PR China Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering(MOE) School of Chemical Engineering and TechnologyTianjin UniversityTianjin300350PR China Collaborative Innovation Center of Chemical Science and Engineering(Tianjin) Tianjin300072PR China

Mineralization catalyzed by carbonic anhydrase(CA)is one of the most promising technologies for capturing CO_(2).In this work,Escherichia coli BL21(DE3)was used as the host,and the N-terminus of ice nucleation protein(INPN)was used as the carrier *** fusion patterns and vectors were used to construct CA surface display systems forα-carbonic anhydrase(HPCA)from Helicobacter pylori 26695 andα-carbonic anhydrase(SazCA)from Sulfurihydrogenibium *** surface display system in which HPCA was fused with INPN via a flexible linker and intermediate repeat sequences showed higher whole-cell enzyme activity,while the enzyme activity of the SazCA expression system was significantly higher than that of the HPCA expression *** pET22b vector with the signal peptide PelB was more suitable for the cell surface display of *** frac-tionation and western-blot analysis indicated that SazCA and INPN were successfully anchored on the cell’s outer membrane as a fusion *** enzyme activity of the surface display strain E-22b-I RL S(11.43 U⋅mL^(−1) OD 600−1)was significantly higher than that of the intracellular expression strain E-22b-S(8.355 U⋅mL^(−1) OD 600−1)under optimized induction *** with free SazCA,E-22b-I RL S had higher thermal and pH *** long-term stability of SazCA was also significantly improved by surface *** the engineered strain and free enzyme were used for CO_(2) mineralization,the amount of CaCO_(3) deposition catalyzed by the strain E-22b-I RL S on the surface(241 mg)was similar to that of the free SazCA and was significantly higher than the intracellular expression strain E-22b-S(173 mg).These results demonstrate that the SazCA surface display strain can serve as a whole-cell biocatalyst for CO_(2) capture and mineralization.

关键词： Carbonic anhydrase cell surface display Enzyme stability CO_(2)mineralization Ice nucleation protein

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surface display of Domain Ⅲ of Japanese Encephalitis Virus E Protein on Salmonella Typhimurium by Using an Ice Nucleation Protein

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Virologica Sinica 2011年第6期26卷 409-417页

作者： Jian-lin Dou Tao Jing Jingojing Fan Zhi-ming Yuan Key Laboratory of Agricultural and Environmental Microbiology Wuhan Institute of Virology Chinese Academy Lanzhou of Sciences Wuhan 430071 China Institute of Pathogenic biology School of Basic Medical Sciences University Lanzhou 730000 China

A bacterial cell surface display technique based on an ice nucleation protein has been employed for the development of live vaccine against viral infection. Due to its ubiquitous ability to invade host cells, Salmonella typhimurium might be a good candidate for displaying viral antigens. We demonstrated the surface display of domain III of Japanese encephalitis virus E protein and the enhanced green fluorescent protein on S. typhimurium BRD509 using the ice nucleation protein. The effects of the motif in the ice nucleation protein on the effective display of integral protein were also investigated. The results showed that display motifs in the protein can target integral foreign protein on the surface of S. typhimurium BRD509. Moreover, recombinant strains with surface displayed viral proteins retained their invasiveness, suggesting that the recombinant S. typhimurium can be used as live vaccine vector for eliciting complete immunogenicity. The data may yield better understanding of the mechanism by which ice nucleation protein displays foreign proteins in the Salmonella strain.

关键词： cell surface display Ice nucleation protein Salmonella typhimurium Japanese encephalitis virus

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