Molecular cloning and characterization of glutamine synthetase, a tegumental protein from Schistosoma japonicum

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	Molecular cloning and characterization of glutamine synthetase, a tegumental protein from Schistosoma japonicum
	Qiu, Chunhui ; Hong, Yang ; Cao, Yan ; Wang, Fei ; Fu, Zhiqiang ; Shi, Yaojun ; Wei, Meimei ; Liu, Shengfa ; Lin, Jiaojiao ; Qiu CH(邱春晖)
刊名	http://dx.doi.org/10.1007/s00436-012-3092-6
	2012-12
关键词	GENE-EXPRESSION ENCHYTRAEUS-JAPONENSIS ESCHERICHIA-COLI REGENERATION METABOLISM INFECTION ENDOTOXIN VACCINES CDNA
英文摘要	National Natural Science Foundation of China [31172315]; Special Fund for Agro-Scientific Research in the Public Interest [200903036]; Glutamine synthetase catalyzes the synthesis of glutamine, providing nitrogen for the production of purines, pyrimidines, amino acids, and other compounds required in many pivotal cellular events. Herein, a full-length cDNA encoding Schistosoma japonicum glutamine synthetase (SjGS) was isolated from 21-day schistosomes. The entire open reading frame of SjGS contains a 1,095-bp coding region corresponding to 364 amino acids with a calculated molecular weight of 40.7 kDa. NCBIP blast shows that the putative amino acid of SjGS contains a classic beta-grasp domain and a catalytic domain of glutamine synthetase. The relative mRNA expression of SjGS was evaluated in 7-, 13-, 21-, 28-, 35-, and 42-day worms of S. japonicum in the final host and higher expression at day 21, and 42 worms were observed. This protein was also detected in worm extracts using Western blot. Immunofluorescence studies indicated that the SjGS protein was mainly distributed on tegument and parenchyma in 28-day adult worms. The recombinant glutamine synthetase with a molecular weight of 45 kDa was expressed in Escherichia coli and purified in its active form. The enzyme activity of the recombinant protein was 3.30 +/- 0.67 U.mu g-1. The enzyme activity was highly stable over a wide range of pH (6-9) and temperature (25-40 A degrees C) under physiological conditions. The transcription of SjGS was upregulated in praziquantel-treated worms at 2-, 4-, and 24-h posttreatment compared with the untreated control. As a first step towards the clarification of the role of glutamine synthetase in schistosome species, we have cloned and characterized cDNAs encoding SjGS in S. japonicum, and the data presented suggest that SjGS is an important molecule in the development of the schistosome.
语种	英语
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/66702]
专题	数学科学－已发表论文
推荐引用方式 GB/T 7714	Qiu, Chunhui,Hong, Yang,Cao, Yan,et al. Molecular cloning and characterization of glutamine synthetase, a tegumental protein from Schistosoma japonicum[J]. http://dx.doi.org/10.1007/s00436-012-3092-6,2012.
APA	Qiu, Chunhui.,Hong, Yang.,Cao, Yan.,Wang, Fei.,Fu, Zhiqiang.,...&邱春晖.(2012).Molecular cloning and characterization of glutamine synthetase, a tegumental protein from Schistosoma japonicum.http://dx.doi.org/10.1007/s00436-012-3092-6.
MLA	Qiu, Chunhui,et al."Molecular cloning and characterization of glutamine synthetase, a tegumental protein from Schistosoma japonicum".http://dx.doi.org/10.1007/s00436-012-3092-6 (2012).