Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid

Chung, Young Bae; Kong, Yoon; Cho, S Y; Yang, Hyun

doi:10.1007/s00436-002-0694-4

Cited by 6 publications

(5 citation statements)

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“…Most of these ligands shared common properties of calcium dependency [ 35 – 37 ] and/or post-translationally modified by glycosylation [ 8 ]. Previous studies have reported that cestode CC bound to calcium binding proteins [ 20 , 23 ] and glycoproteins [ 21 , 23 ]. Calcium-related biochemical properties of TsMFas1 and TsMFas2 proteins were not examined in this study.…”

Section: Discussionmentioning

confidence: 99%

Fasciclin-calcareous corpuscle binary complex mediated protein-protein interactions in Taenia solium metacestode

et al. 2017

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BackgroundNeurocysticercosis (NC) caused by Taenia solium metacestode (TsM) is a serious neurological disease of global concern. Diverse bioactive molecules involved in the long-term survival of TsM might contribute to disease progression. Fasciclin (Fas) is an extracellular protein that mediates adhesion, migration and differentiation of cells by interacting with other molecules. We hypothesized that TsMFas might bind to calcareous corpuscle (CC) through its adhesive property and participate in crucial protein-protein interactions, thus contributing to the creation of a symbiotic interactome network.MethodsTwo paralogous TsMFas (TsMFas1 and TsMFas2) were isolated, and their molecular properties were characterized. The co-localization pattern of TsMFas1 and TsMFas2 with CC was determined. CC-TsMFas binary complex was generated by incubating CC with recombinant proteins (rTsMFas1 and 2). In vitro binding assay of CC-rTsMFas1 or CC-rTsMFas2 binary complex with TsM cellular proteins extracted from scolex and neck was conducted. Their binding partners were identified through proteomic analysis. Integrated protein-protein interaction networks were established.Results TsMFas1 (6072 bp long) was composed of 15 exons (841 amino acid polypeptide) interrupted by 14 introns. TsMFas2 (5201 bp long) comprised of 11 exons (597 amino acids) and 10 intervening introns. These proteins displayed 22% amino acid sequence identity to each other, but tightly conserved Fas-related domains. Several isoforms of Fas1 and Fas2 proteins might have been expressed through post-translational modifications. They showed adhesion activity with other cells. TsMFas proteins were largely distributed in parenchymal regions of the scolex and bladder wall. These molecules were co-localized with CC, a unique organelle found in platyhelminths. Subsequent proteome analysis of CC-Fas binary complex mediated protein-protein interactions revealed seven protein ligands in the TsM cellular proteins. Their functions were mainly segregated into carbohydrate metabolism (enolase, phosphoenolpyruvate carboxykinase, phosphoglycerate kinase and glyceraldehyde 3-phosphate dehydrogenase) and cytoskeleton/cellular motility (actin, paramyosin and innexin nuc-9). Those proteins had direct (physical) and/or indirect (functional) relationships along with their biochemical properties and biological roles.ConclusionProtein repertoires strongly suggest that TsMFas and CC may symbiotically mediate protein-protein interactions during biological processes to maintain efficacious homeostatic functions and ensure the prolonged survival of TsM in the host.Electronic supplementary materialThe online version of this article (10.1186/s13071-017-2359-2) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Fasciclin-calcareous corpuscle binary complex mediated protein-protein interactions in Taenia solium metacestode

et al. 2017

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“…It has been shown for other species that, aside from the various functions ascribed to calcareous corpuscles, e.g. osmoregulation and protection from abnormal calcification (28), these structures have the capacity of binding proteins (29,30). Whether they behave as a reservoir for EgA31 cannot be decided with the present observations.…”

Section: Discussionmentioning

confidence: 99%

The Echinococcus granulosus antigen EgA31: localization during development and immunogenic properties

Saboulard

Lahmar²,

Pétavy

et al. 2003

Parasite Immunology

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EgA31 is a fibrillar protein from Echinococcus granulosus that behaves as a potent antigen during infestation of dogs. The localization of this antigen during development of the parasite was investigated by immunohistochemistry in optical and electron microscopy. The protein is mostly abundant in the microtriches and subtegumental cells of the adult, whereas it is absent from protoscolex microtriches. Eggs, the periphery of calcareous corpuscles, and the germinal layer were other sites of accumulation. Immunogenicity of different domains of the protein was assessed during experimental infection of dogs. It was shown that the polypeptide encoded by the Pst I-Hind III fragment of the complete cDNA is the most antigenic during the infection. The uses of such polypeptide for infection diagnosis and as a candidate vaccine protein are discussed.

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“…Formation of CC has been proposed as a mechanism for protecting cysticerci from calcification [79]. The CC represent about 10% of the dry weight of total larval tissue [82]. It has been estimated that in aged T. s o l i u m cysticerci, calcareous corpuscles can represent up to 41% of the dry weight [81,82].…”

Section: The Calcareous Corpuscles As a Final Deposit For Host Proteinsmentioning

confidence: 99%

To Be or Not to Be a Tapeworm Parasite: That Is the Post-Genomic Question in Taenia solium Cysticercosis

Ríos-Valencia¹,

Navarrete‐Perea²,

Calderón-Gallegos³

et al. 2021

Current State of the Art in Cysticercosis and Neurocysticercosis

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Cestode parasites rely on their host to obtain their nutrients. Elucidation of tapeworm genomes has shown a remarkable reduction in the coding of multiple enzymes, particularly those of anabolic pathways. Previous findings showed that 10–13% of the proteins found in the vesicular fluid of Taenia solium cysticerci are of host origin. Further proteomic characterization allowed identification of 4,259 different proteins including 891 of host origin in the parasite’s protein lysates. One explanation for this high abundance and diversity of host proteins in the parasite lysates is related to the functional exploitation of host proteins by cysticerci. Supporting this concept is the uptake of host haptoglobin and hemoglobin by the parasite, as a way to acquire iron. Surprisingly, internalized host proteins are minimally degraded by the parasite physiological machinery. Additional proteomic analysis demonstrated that these host proteins become part of the organic matrix of calcareous corpuscles; as 60–70% of the protein content are host proteins. In this review, a collection of available genomic and proteomic data for taeniid cestodes is assembled, the subject of the use and processing of host proteins is particularly addressed; a sketchy and unique cell physiological profile starts to emerge for these parasitic organisms.

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Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid

Cited by 6 publications

References 7 publications

Fasciclin-calcareous corpuscle binary complex mediated protein-protein interactions in Taenia solium metacestode

Fasciclin-calcareous corpuscle binary complex mediated protein-protein interactions in Taenia solium metacestode

The Echinococcus granulosus antigen EgA31: localization during development and immunogenic properties

To Be or Not to Be a Tapeworm Parasite: That Is the Post-Genomic Question in Taenia solium Cysticercosis

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