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Characterization of a Novel Glutamine Synthetase From Trichinella spiralis and Its Participation in Larval Acid Resistance, Molting, and Development.
Zhuo, Tong Xu; Wang, Zhen; Song, Yan Yan; Yan, Shu Wei; Liu, Ruo Dan; Zhang, Xi; Wang, Zhong Quan; Cui, Jing.
Afiliación
  • Zhuo TX; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Wang Z; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Song YY; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Yan SW; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Liu RD; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Zhang X; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Wang ZQ; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
  • Cui J; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou, China.
Front Cell Dev Biol ; 9: 729402, 2021.
Article en En | MEDLINE | ID: mdl-34616735
Trichinella spiralis is a major foodborne parasite worldwide. After the encapsulated muscle larvae (ML) in meat are ingested, the ML are liberated in the stomach of the host and activated into intestinal infectious larvae (IIL), which develop into adult worm after molting four times. A novel glutamine synthetase (TsGS) was identified from T. spiralis IIL at 10 h post-infection, but its biological role in T. spiralis life cycle is not clear. The aim of this study was to investigate the biological characteristics of TsGS and its functions in larval acid resistance, molting, and development. TsGS has a glutamine synthetase (GS) catalytic domain. Complete TsGS sequence was cloned and expressed in Escherichia coli BL21. rTsGS has good immunogenicity. qPCR and Western blotting showed that TsGS was highly expressed at IIL stage, and immunofluorescence revealed that TsGS was principally localized at the cuticle and intrauterine embryos of this nematode. rTsGS has enzymatic activity of natural GS to hydrolyze the substrate (Glu, ATP, and NH4 +). Silencing of TsGS gene significantly reduced the IIL survival at pH 2.5, decreased the IIL burden, and impeded larval molting and development. The results demonstrated that TsGS participates in T. spiralis larval acid resistance, molting and development, and it might be a candidate vaccine target against Trichinella molting and development.
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Texto completo: 1 Base de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Revista: Front Cell Dev Biol Año: 2021 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Revista: Front Cell Dev Biol Año: 2021 Tipo del documento: Article