A novel tegumental protein 31.8 kDa of Clonorchis sinensis: sequence analysis, expression, and immunolocalization

Huang, Yan; Zhou, Zhenwen; Hu, Xuchu; Wei, Qian; Xu, Jin; Wu, Zhongdao; Yu, Xinbing

doi:10.1007/s00436-007-0728-z

Cited by 30 publications

(17 citation statements)

References 15 publications

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“…Due to their accessibility on adult worms, tegumental proteins are regarded as target molecules for vaccines (Loukas et al 2007). To date, four genes encoding C. sinensis tegumental proteins have been identified and characterized (Chen et al 2011;Huang et al 2007;Zhou et al 2007;Zhou et al 2008). The current study was carried out to identify and characterize a novel 21.6-kDa C. sinensis tegumental protein (CsTegu21.6) from the expressed sequence tag (EST) database of C. sinensis using bioinformatic analysis.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis

et al. 2011

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Tegumental proteins form a membrane-bound outer surface and are thus involved in host-parasite interactions and parasite survival. A complementary DNA clone encoding a novel 21.6-kDa tegumental protein (CsTegu21.6, accession number JF911532) was identified in a sequence library for the adult Clonorchis sinensis liver fluke. The complete coding sequence was 564 bp and encoded a protein of 188 amino acids. A BLASTX search revealed identities from 43 to 47% with previously identified tegumental proteins in C. sinensis and other helminthic parasites. Multiple alignment of the amino acids of CsTegu21.6 with those of four other C. sinensis tegumental proteins, CsTegu21.1, CsTegu22.3, CsTegu20.8 and CsTegu31.8, revealed pair-wise sequence identities ranging from 24 to 31.8%. A calcium-binding EF-hand domain containing a basic helix-loop-helix structure at the N terminus and a dynein light chain domain at the C terminus were found in CsTegu21.6; these motifs are common in tegumental proteins. CsTegu21.6 was specifically observed on the tegument of adult worms using immunolocalization analysis.

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Section: Introductionmentioning

confidence: 99%

Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis

et al. 2011

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“…This species expresses 13 family members, some of which have been shown to elicit IgE-mediated immune responses in the host (Fitzsimmons, et al, 2012, Fitzsimmons, et al, 2007, Webster, et al, 1997. Proteins from this family have also been identified and characterised from other species in the genus Schistosoma, from the Chinese liver fluke Clonorchis sinensis (Huang, et al, 2007, Kim, et al, 2012, Senawong, et al, 2012, Subpipattana, et al, 2012, Vichasri-Grams, et al, 2006, the giant liver fluke Fasciola gigantica and the carcinogenic liver fluke, Opisthorchis viverrini (Fitzsimmons, et al, 2004, Li, et al, 2000, Santiago, et al, 1998, Waine, et al, 1994, Xu, et al, 2014, Zhang, et al, 2012.…”

Section: Introductionmentioning

confidence: 99%

“…While many of the proteins have been localised to the tegument of the worm, their in vivo functions have not been elucidated (Fitzsimmons, et al, 2012, Havercroft, et al, 1990, Huang, et al, 2007, Kim, et al, 2012, Lopes, et al, 2009, Mohamed, et al, 1998, Subpipattana, et al, 2012, Xu, et al, 2014, Zhang, et al, 2012. From the available data it is evident that, despite clear sequence similarities, differences exist between the proteins at the biochemical level.…”

Section: Introductionmentioning

confidence: 99%

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Cheung

Thomas

Timson

2016

Experimental Parasitology

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FH22 has been previously identified as a calcium-binding protein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EFhand containing N-terminal domain with a C-terminal dynein light chainlike domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site. Native gel electrophoresis demonstrated that the protein binds both calcium and manganese ions, but not cadmium, magnesium, strontium, barium, cobalt, copper(II), iron (II), nickel, zinc, lead or potassium ions. Calcium ion binding alters the conformation of the protein and increases its stability towards thermal denaturation. FhCaBP1 is a dimer in solution and calcium ions have no detectable effect on the protein's ability to dimerise. FhCaBP1 binds to the calmodulin antagonists trifluoperazine and chlorpromazine. Overall, the FhCaBP1's biochemical properties are most similar to FhCaBP2 a fact consistent with the close sequence and predicted structural similarity between the two proteins. properties are most similar to FhCaBP2 a fact consistent with the close sequence and predicted structural similarity between the two proteins.

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“…Oral administration of the CsTP20.8 protein provoked specific IgA production, detected in feces [103,104]. Furthermore, a tegumental protein of 31.8 kDa (CsTP31.8) was immunolocalized to the tegument of adult C. sinensis, and has been suggested to be an antigenic protein for the serodiagnosis of clonorchiasis [105].…”

Section: Tegumental Proteinsmentioning

confidence: 98%

Functional Genes and Proteins of Clonorchis sinensis

Kim

Hong

2009

Korean J Parasitol

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During the past several decades, researches on parasite genetics have progressed from biochemical and serodiagnostic studies to protein chemistry, molecular biology, and functional gene studies. Nowadays, bioinformatics, genomics, and proteomics approaches are being applied by Korean parasitology researchers. As for Clonorchis sinensis, investigations have been carried out to identify its functional genes using forward and reverse genetic approaches and to characterize the biochemical and biological properties of its gene products. The authors review the proteins of cloned genes, which include antigenic proteins, physiologic and metabolic enzymes, and the gene expression profile of Clonorchis sinensis. CHROMOSOMES AND GEOGRAPHICAL ISOLATESC. sinensis has 2n = 56 chromosomes, where n consists of 8 large and 20 small chromosomes. C. sinensis geographical isolates collected in Korea and northeastern China (Liaoning Province) have all demonstrated the same chromosome number, but different karyotypes. Specifically, Korean isolates have 3 metacentric and 1 meta-/submetacentric pairs, whereas Chinese isolates have 2 and 2 pairs, respectively. The 2 isolates have same number, 16 and 8, of submetacentric and subtelomeric pairs [13].Genetic relationships between geographical isolates have been studied by employing sequence analyses of nuclear ribosomal DNA (18S, internal transcribed spacer 1 and 2; ITS1 and ITS2) and mitochondrial DNA (cytochrome c oxidase subunit 1 [CO-1]). C. sinensis Korean isolates collected in Kimhae city were compared with Chinese isolates collected in Shenyang, Liaoning and Nanning, and Guangxi provinces. The geographical isolates were nearly identical in terms of nuclear ribosomal and mitochondrial DNA sequences, and revealed no more than a 1% sequence difference between Korean and Chinese isolates [14][15][16][17]. Isozyme electrophoresis had been used to study trematode systematics, and isozymes of the Korean and Chinese isolates show homozygous monomorphic banding patterns. Furthermore, alpha-glycerophosphate dehydrogenase produced a unique band pattern and was found to differentiate geographical isolates of C. sinensis [14]. However, in C. sinensis, intraspecific genetic variations among geographical isolates in the SinoKorea region appear minimal.As compared with O. viverrini, C. sinensis ITS2 revealed 95% identity and differences at 28 nucleotide points. Furthermore, the mitochondrial CO1 gene of O. viverrrini was found to be 96% identical with that of C. sinensis. Even a different genus in the same family Opisthorchidae, namely, O viverrrini appears to be genetically close to C. sinensis [17].

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A novel tegumental protein 31.8 kDa of Clonorchis sinensis: sequence analysis, expression, and immunolocalization

Cited by 30 publications

References 15 publications

Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis

Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Functional Genes and Proteins of Clonorchis sinensis

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