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논문 기본 정보

자료유형
학술저널
저자정보
Xu Tao (Department of Clinical Laboratory School of Laboratory Medicine Bengbu Medical College Bengbu Anhui) Li Minying (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a) Wang Chutong (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a) Yuan Meili (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a) Chang Xianyou (The Infectious Disease Hospital of Bengbu City Bengbu Anhui 233000 P.R. China) Qian Zhongqing (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a) Li Baiqing (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a) Sun Meiqun (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a) Wang Hongtao (Anhui Province Key Laboratory of Immunology in Chronic Diseases Anhui Key Laboratory of Infection a)
저널정보
한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제31권 제11호
발행연도
2021.11
수록면
1,583 - 1,590 (8page)
DOI
10.4014/jmb.2106.06006

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Studies have demonstrated that PE_PGRS45 is constitutively expressed under various environmental conditions (such as nutrient depletion, hypoxia, and low pH) of the in vitro growth conditions examined, indicating that PE_PGRS45 protein is critical to the basic functions of Mycobacterium tuberculosis. However, there are few reports about the biochemical function and pathogenic mechanism of PE_PGRS45 protein. The fact that this M. tuberculosis gene is not easily expressed in E. coli may be mainly due to the high content of G+C and the use of unique codons. Fusion tags are indispensable tools used to improve the soluble expression of recombinant proteins and accelerate the characterization of protein structure and function. In the present study, His6, Trx, and His6-MBP were used as fusion tags, but only MBP-PE_PGRS45 was expressed solubly. The purification using His6-MBP tag-specific binding to the Ni column was easy to separate after the tag cleavage. We used the purified PE_PGRS45 to immunize New Zealand rabbits and obtained anti- PE_PGRS45 serum. We found that the titer of polyclonal antibodies against PE_PGR45 was higher than 1:256000. The result shows that purified PE_PGRS45 can induce New Zealand rabbits to produce high-titer antibodies. In conclusion, the recombinant protein PE_PGRS45 was successfully expressed in E. coli and specific antiserum was prepared, which will be followed by further evaluation of these specific antigens to develop highly sensitive and specific diagnostic tests for tuberculosis.
#Mycobacterium tuberculosis #Rv2615c #PE_PGRS45 protein #codon optimization #soluble expression #polyclonal antibody

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참고문헌 (31)

참고문헌 신청
Qian J / 2020 / Role of the PE/PPE family in host-pathogen interactions and prospects for anti-tuberculosis vaccine and diagnostic tool design / Front. Cell Infect. Microbiol 10:594288 google schola Wang Y / 2021 / Systematic evaluation of Mycobacterium tuberculosis proteins for antigenic properties identifies Rv1485 and Rv1705c as potential protective subunit vaccine candidates / Infect. Immun 89:e00585~20 google schola Global tuberculosis Report 2020 google schola Glaziou P / 2020 / Predicted impact of the COVID-19 pandemic on global tuberculosis deaths in 2020 / medRxiv 2020.04.28.20079582 google schola Cole ST / 1998 / Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence / Nature 393:537~544 google schola

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