Proteomic analysis of excretory secretory products from Clonorchis sinensis adult worms: molecular characterization and serological reactivity of a excretory–secretory antigen-fructose-1,6-bisphosphatase

Zheng, Min; Hu, Kunhua; Liu, Wei; Hu, Xuchu; Hu, Fengyu; Huang, Lisi; Wang, Peng; Hu, Yue; Huang, Yan; Li, Wenfang; Liang, Chi; Yin, Xinhua; He, Qing‐Yu; Yu, Xinbing

doi:10.1007/s00436-011-2316-5

Cited by 53 publications

(40 citation statements)

References 34 publications

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“…FBPase has been described among components of excretory secretory products from Clonorchis sinensis adult worms and indicate that FBPase may serve as a marker in diagnosing clonorchiasis-associated hepatic fibrosis [57] . In addition, FBPase has also been identified as a bio-marker for assessing damage to the proximal renal tubules [58] .…”

Section: Future Directionsmentioning

confidence: 99%

Vacuole import and degradation pathway: Insights into a specialized autophagy pathway

Alibhoy¹

2011

WJBC

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Glucose deprivation induces the synthesis of pivotal gluconeogenic enzymes such as fructose-1,6-bisphosphatase, malate dehydrogenase, phosphoenolpyruvate carboxykinase and isocitrate lyase in Saccharomyces cerevisiae . However, following glucose replenishment, these gluconeogenic enzymes are inactivated and degraded. Studies have characterized the mechanisms by which these enzymes are inactivated in response to glucose. The site of degradation of these proteins has also been ascertained to be dependent on the duration of starvation. Glucose replenishment of short-term starved cells results in these proteins being degraded in the proteasome. In contrast, addition of glucose to cells starved for a prolonged period results in these proteins being degraded in the vacuole. In the vacuole dependent pathway, these proteins are sequestered in specialized vesicles termed vacuole import and degradation (Vid). These vesicles converge with the endocytic pathway and deliver their cargo to the vacuole for degradation. Recent studies have identified that internalization, as mediated by actin polymerization, is essential for delivery of cargo proteins to the vacuole for degradation. In addition, components of the target of rapamycin complex 1 interact with cargo proteins during glucose starvation. Furthermore, Tor1p dissociates from cargo proteins following glucose replenishment. Future studies will be needed to elaborate on the importance of internalization at the plasma membrane and the subsequent import of cargo proteins into Vid vesicles in the vacuole dependent degradation pathway.

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Section: Future Directionsmentioning

confidence: 99%

Vacuole import and degradation pathway: Insights into a specialized autophagy pathway

Alibhoy¹

2011

WJBC

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“…Clonorchis sinensis triosephosphate isomerase (CsTIM) has been identified as a component of Cl. sinensis excretory/secretory products (CsESPs) (Zheng et al 2011), which are generally believed to play key roles in host-parasite interaction in previous studies (Mulvenna et al 2010 andXu et al 2013). However, the biochemical characterizations of CsTIM remain obscure.…”

Section: Introductionmentioning

confidence: 99%

Molecular identification, immunolocalization, and characterization of Clonorchis sinensis triosephosphate isomerase

Zhou

Liao

et al. 2015

Parasitol Res

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Clonorchis sinensis triosephosphate isomerase (CsTIM) is a key regulatory enzyme of glycolysis and gluconeogenesis, which catalyzes the interconversion of glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. In this study, the biochemical characterizations of CsTIM have been examined. A full-length complementary DNA (cDNA; Cs105350) sequence encoding CsTIM was obtained from our C. sinensis cDNA library. The open reading frame of CsTIM contains 759 bp which encodes 252 amino acids. The amino acid sequence of CsTIM shares 60-65% identity with other species. Western blot analysis displayed that recombinant CsTIM (rCsTIM) can be probed by anti-rCsTIM rat serum and anti-C. sinensis excretory/secretory products (anti-CsESPs) rat serum. Quantitative reverse transcription (RT)-PCR and western blotting analysis revealed that CsTIM messenger RNA (mRNA) and protein were differentially expressed in development cycle stages of the parasite, including adult worm, metacercaria, excysted metacercaria, and egg. In addition, immunolocalization assay showed that CsTIM was located in the seminal vesicle, eggs, and testicle. Moreover, rCsTIM exhibited active enzyme activity in catalytic reactions. The Michaelis constant (K m) of rCsTIM was 0.33 mM, when using glyceraldehyde 3-phosphate as the substrate. The optimal temperature and pH of CsTIM were 37 °C and 7.5-9.5, respectively. Collectively, these results suggest that CsTIM is an important protein involved in glycometabolism, and CsTIM possibly take part in many biological functions in the growth and development of C. sinensis.

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“…There have been several attempts to identify potential drug targets by genomic [5] and proteomic approach [6]. Recently, a secretory protein from the parasite Clonorchis sinensis has been established to be the causative agent of hepatic fibrosis and is being advocated as a potential drug target [7].…”

Section: Introductionmentioning

confidence: 99%

Structural analysis of secretory phospholipase A2 from Clonorchis sinensis: therapeutic implications for hepatic fibrosis

et al. 2012

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Hepatic fibrosis is a common complication of the infection by the parasite, Clonorchis sinensis. There is a high incidence of this disease in the Asian countries with an increased risk of conversion to cancer. A secretory phospholipase A(2) (PLA(2)) enzyme from the parasite is implicated in the pathology. This is an attractive drug target in the light of extensive structural characterization of this class of enzyme. In this study, the structure of the enzyme was modeled based on its sequence homology to the group III bee venom PLA(2). On analysis, the overall structure essentially is comprised of three helices, two sets of β-wings and an elongated C-terminal extension. The structure is stabilized by four disulfide bonds. The structure is comprised of a calcium binding loop, active site and a substrate binding hydrophobic channel. The active site of the enzyme shows the classical features of PLA(2) with the participation of the three residues: histidine-aspartic acid-tyrosine in hydrogen bond formation. This is an interesting variation from the house keeping group III PLA(2) enzyme of human which has a histidine-aspartic acid and phenylalanine arrangement at the active site. This difference is therefore an important structural parameter that can be exploited to design specific inhibitor molecules against the pathogen PLA(2). Likewise, there are certain unique structural features in the hydrophobic channel and the putative membrane binding surface of the PLA(2) from Clonorchis sinensis that not only help understand the mechanism of action but also provide knowledge for a targeted therapy of liver fibrosis caused by the parasite.

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Proteomic analysis of excretory secretory products from Clonorchis sinensis adult worms: molecular characterization and serological reactivity of a excretory–secretory antigen-fructose-1,6-bisphosphatase

Cited by 53 publications

References 34 publications

Vacuole import and degradation pathway: Insights into a specialized autophagy pathway

Vacuole import and degradation pathway: Insights into a specialized autophagy pathway

Molecular identification, immunolocalization, and characterization of Clonorchis sinensis triosephosphate isomerase

Structural analysis of secretory phospholipase A2 from Clonorchis sinensis: therapeutic implications for hepatic fibrosis

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