Proteomic analysis of differentially expressed proteins in the three developmental stages of Trichinella spiralis

Liu, J.Y.; Zhang, N.Z.; Li, W.H.; Li, L.; Yan, Hong‐Bin; Qu, Zigang; Li, T.T.; Cui, Jiangkuan; Yang, Yongqing; Jia, Wan‐Zhong; Fu, Bao‐Quan

doi:10.1016/j.vetpar.2016.06.021

Cited by 28 publications

(29 citation statements)

References 31 publications

(38 reference statements)

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“…The TsSP-ZH68 belongs to peptidase S1A, chymotrypsin family, and chymotrypsin is a digestive enzyme of pancreatic juice in the duodenum where it carries out proteolysis, the breakdown of proteins and polypeptides (Wilcox, 1970). Serine proteases with chymotrypsin-like, elastase-like or trypsin-like activities are the most abundant protease of T. spiralis ES products or crude extract (Todorova and Stoyanov, 2000; Wang et al, 2014; Yang et al, 2015b; Liu J.Y. et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

“…Trichinella spiralis muscle larvae (ML) excretory-secretory (ES) antigens, recommended by the International Commission on Trichinellosis (ICT), are the most commonly used serodiagnostic antigens for trichinellosis (Gamble et al, 2004), but the specific antibodies against the ML ES antigens are usually negative during early stage of Trichinella infection (Cui et al, 2015), possibly because the majority of ML ES antigens are the stage-specific and not recognized by specific antibodies produced during the intestinal phase (Liu J.Y. et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

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Proteomic Analysis of Trichinella spiralis Adult Worm Excretory-Secretory Proteins Recognized by Sera of Patients with Early Trichinellosis

et al. 2017

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The most commonly used serodiagnostic antigens for trichinellosis are the excretory-secretory (ES) antigens from T. spiralis muscle larvae (ML), but the specific antibodies against the ML ES antigens are usually negative during early stage of Trichinella infection. The recent studies demonstrated that T. spiralis adult worm (AW) antigens were recognized by mouse or swine infection sera on Western blot as early as 7–15 days post-infection (dpi), the AW antigens might contain the early diagnostic markers for trichinellosis. The purpose of this study was to screen early diagnostic antigens in T. spiralis AW ES proteins recognized by sera of early patients with trichinellosis. T. spiralis AW were collected at 72 h post-infection (hpi), and their ES antigens were analyzed by SDS-PAGE and Western blot. Our results showed that 5 protein bands (55, 48–50, 45, 44, and 36 kDa) were recognized by sera of early patients with trichinellosis collected at 19 dpi, and were subjected to shotgun LC–MS/MS and bioinformatics analyses. A total of 185 proteins were identified from T. spiralis protein database, of which 116 (67.2%) proteins had molecular weights of 30∼60 kDa, and 125 (67.6%) proteins with pI 4–7. Bioinformatic analyses showed that the identified proteins have a wide diversity of biological functions (binding of nucleotides, proteins, ions, carbohydrates, and lipids; hydrolase, transferase, and oxidoreductase, etc.). Several enzymes (e.g., adult-specific DNase II, serine protease and serine protease inhibitor) could be the invasion-related proteins and early diagnostic markers for trichinellosis. Moreover, recombinant T. spiralis serine protease (rTsSP-ZH68) was expressed in E. coli and its antigenicity was analyzed by Western blot with the early infection sera. The rTsSP-ZH68 was recognized by sera of infected mice at 8–10 dpi and sera of early patients with trichinellosis at 19 dpi. T. spiralis AW proteins identified in this study, especially serine protease, are the promising early diagnostic antigens and vaccine candidates for trichinellosis.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of Trichinella spiralis Adult Worm Excretory-Secretory Proteins Recognized by Sera of Patients with Early Trichinellosis

et al. 2017

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“…In recent years, the genome, transcriptome, epigenome, and proteome of T. spiralis have been reported and released in public databases, providing a greater understanding of the molecular basis of T. spiralis biology, host–parasite interactions, and pathogenesis ( Mitreva et al, 2011 ; Gao et al, 2012 ; Liu et al, 2012 , 2016 ). However, to the best of our knowledge, no post-translational modifications (PTMs), which occur during or after protein biosynthesis, have been described in T. spiralis , limiting further functional studies.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive Proteomic Analysis of Lysine Acetylation in the Foodborne Pathogen Trichinella spiralis

et al. 2018

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Lysine acetylation is a dynamic and highly conserved post-translational modification that plays a critical role in regulating diverse cellular processes. Trichinella spiralis is a foodborne parasite with a considerable socio-economic impact. However, to date, little is known regarding the role of lysine acetylation in this parasitic nematode. In this study, we utilized a proteomic approach involving anti-acetyl lysine-based enrichment and highly sensitive mass spectrometry to identify the global acetylated proteome and investigate lysine acetylation in T. spiralis. In total, 3872 lysine modification sites were identified in 1592 proteins that are involved in a wide variety of biological processes. Consistent with the results of previous studies, a large number of the acetylated proteins appear to be involved in metabolic and biosynthetic processes. Interestingly, according to the functional enrichment analysis, 29 acetylated proteins were associated with phagocytosis, suggesting an important role of lysine acetylation in this process. Among the identified proteins, 15 putative acetylation motifs were detected. The presence of serine downstream of the lysine acetylation site was commonly observed in the regions surrounding the sites. Moreover, protein interaction network analysis revealed that various interactions are regulated by protein acetylation. These data represent the first report of the acetylome of T. spiralis and provide an important resource for further explorations of the role of lysine acetylation in this foodborne pathogen.

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“…In recent years, proteomic analysis has become a useful technique for detection and identification of somatic proteins or ESPs from different stages, sexes, hosts, or conditions of parasitic helminths including A. cantonensis , 18 , 24 Trichinella spiralis , 25 , 26 Dirofilaria immitis , 27 Schistosoma mansoni , 28 Schistosoma japonicum , 29 and Echinococcus granulosus . 30 Identification of significant ESP molecules is a good strategy to determine the host-parasite interaction, and may facilitate novel ideas for disease treatment and diagnosis.…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of excretory-secretory products from young adults of Angiostrongylus cantonensis

Chen

Cheng

et al. 2019

Mem. Inst. Oswaldo Cruz

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BACKGROUND Angiostrongyliasis is caused by the nematode Angiostrongylus cantonensis and can lead to eosinophilic meningitis and meningoencephalitis in humans. The young adult worms play central pathogenic roles in the central nervous system (CNS); however, the underlying mechanism is unclear. Excretory-secretory products (ESPs) are good investigation targets for studying the relationship between a host and its parasite. OBJECTIVES We aimed to profile, identify, and characterise the proteins in the ESPs of A. cantonensis young adults. METHODS The ESPs of young adult worms were collected from culture medium after incubation ranging from 24 to 96 h. Proteomic and bioinformatics analyses were performed to characterise the ESPs. FINDINGS A total of 51 spots were identified, and the highly expressed proteins included two protein disulphide isomerases, one calreticulin, and three uncharacterised proteins. Subsequently, approximately 254 proteins were identified in the ESPs of A. cantonensis young adults via liquid chromatography-mass spectrometry (LC-MS/MS) analysis, and these were further classified according to their characteristics and biological functions. Finally, we identified the immunoreactive proteins from a reference map of ESPs from A. cantonensis young adults. Approximately eight proteins were identified, including a protein disulphide isomerase, a putative aspartic protease, annexin, and five uncharacterised proteins. The study established and identified protein reference maps for the ESPs of A. cantonensis young adults. MAIN CONCLUSIONS The identified proteins may be potential targets for the development of diagnostic or therapeutic agents for human angiostrongyliasis.

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Proteomic analysis of differentially expressed proteins in the three developmental stages of Trichinella spiralis

Cited by 28 publications

References 31 publications

Proteomic Analysis of Trichinella spiralis Adult Worm Excretory-Secretory Proteins Recognized by Sera of Patients with Early Trichinellosis

Proteomic Analysis of Trichinella spiralis Adult Worm Excretory-Secretory Proteins Recognized by Sera of Patients with Early Trichinellosis

Comprehensive Proteomic Analysis of Lysine Acetylation in the Foodborne Pathogen Trichinella spiralis

Proteomic analysis of excretory-secretory products from young adults of Angiostrongylus cantonensis

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