Mesocestoides corti (syn. vogae, cestoda): Characterization of genes encoding cysteine-rich secreted proteins (CRISP)

Britos, Leticia; Lalanne, Ana I.; Castillo, Estela; Cota, Germán; Señorale, Mario; Marı́n, Mónica

doi:10.1016/j.exppara.2006.11.008

Cited by 9 publications

(5 citation statements)

References 31 publications

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“…For this review, and according to our previous naming convention (Chalmers et al 2008), we have decided to refer to these platyhelminth proteins as the Venom Allergen-Like (VAL) family. The first published report of platyhelminth VAL family members originated from investigations on the cestode Mesocestoides corti – a mouse model for host/cestode relationships (Britos et al 2007). After serendipitously discovering a VAL family member while searching for homeobox containing genes, Britos et al (2007) amplified 4 different VAL transcripts from the larval parasite life stage (tetrathyridia).…”

Section: Published Studies On Platyhelminth Val Proteinsmentioning

confidence: 99%

“…The first published report of platyhelminth VAL family members originated from investigations on the cestode Mesocestoides corti – a mouse model for host/cestode relationships (Britos et al 2007). After serendipitously discovering a VAL family member while searching for homeobox containing genes, Britos et al (2007) amplified 4 different VAL transcripts from the larval parasite life stage (tetrathyridia). Due to strong sequence similarity to human CRISP proteins, the authors named these VAL transcripts McCrisp1–4 (Table 1).…”

Section: Published Studies On Platyhelminth Val Proteinsmentioning

confidence: 99%

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Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum

Chalmers

Hoffmann

2012

Parasitology

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SUMMARYDuring platyhelminth infection, a cocktail of proteins is released by the parasite to aid invasion, initiate feeding, facilitate adaptation and mediate modulation of the host immune response. Included amongst these proteins is the Venom Allergen-Like (VAL) family, part of the larger sperm coating protein/Tpx-1/Ag5/PR-1/Sc7 (SCP/TAPS) superfamily. To explore the significance of this protein family during Platyhelminthes development and host interactions, we systematically summarize all published proteomic, genomic and immunological investigations of the VAL protein family to date. By conducting new genomic and transcriptomic interrogations to identify over 200 VAL proteins (228) from species in all 4 traditional taxonomic classes (Trematoda, Cestoda, Monogenea and Turbellaria), we further expand our knowledge related to platyhelminth VAL diversity across the phylum. Subsequent phylogenetic and tertiary structural analyses reveal several class-specific VAL features, which likely indicate a range of roles mediated by this protein family. Our comprehensive analysis of platyhelminth VALs represents a unifying synopsis for understanding diversity within this protein family and a firm context in which to initiate future functional characterization of these enigmatic members.

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Section: Published Studies On Platyhelminth Val Proteinsmentioning

confidence: 99%

Section: Published Studies On Platyhelminth Val Proteinsmentioning

confidence: 99%

Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum

Chalmers

Hoffmann

2012

Parasitology

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“…For example, Kunitz is identified in the transcriptome of Echinococcus granulosus and has been shown to interfere with host physiological processes during the initial stages of infection [ 59 ]. In addition, CRISP is thought to play an important role in the development and parasite adaptation of cestodes [ 60 ]. Metalloproteinases have been identified in ectoparasitic wasps with abilities to manipulate host development [ 61 ].…”

Section: Discussionmentioning

confidence: 99%

Transcriptomic Insights into the Diversity and Evolution of Myxozoa (Cnidaria, Endocnidozoa) Toxin-like Proteins

et al. 2022

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Myxozoa is a speciose group of endoparasitic cnidarians that can cause severe ecological and economic effects. Their cnidarian affinity is affirmed by genetic relatedness and the presence of nematocysts, historically called “polar capsules”. Previous studies have revealed the presence of toxin-like proteins in myxozoans; however, the diversity and evolution of venom in Myxozoa are not fully understood. Here, we performed a comparative analysis using the newly sequenced transcriptomes of five Myxobolidae species as well as some public datasets. Toxin mining revealed that myxozoans have lost most of their toxin families, while most species retained Kunitz, M12B, and CRISP, which may play a role in endoparasitism. The venom composition of Endocnidozoa (Myxozoa + Polypodium) differs from that of free-living cnidarians and may be influenced by ecological and environmental factors. Phylogenetic analyses showed that toxin families of myxozoans and free-living cnidarians were clustered into different clades. Selection analyses showed that purifying selection was the dominant evolutionary pressure in toxins, while they were still influenced by episodic adaptive selection. This suggests that the potency or specificity of a particular toxin or species might increase. Overall, our findings provide a more comprehensive framework for understanding the diversity and evolution of Myxozoa venoms.

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“…Immediately after extraction from mice, Tt were cultured for five days in RPMI-1640 (Sigma-Aldrich, St. Louis, USA) and 10% foetal bovine serum, followed by one day of culture without serum, according to Britos and coworkers [24] . Some larvae were then incubated with 0.2 µM BODIPY FL C 16 for 15 min at 37°C and others with 0.2 µM MitoTracker Orange CMTMRos for 15 min at 37°C.…”

Section: Methodsmentioning

confidence: 99%

Towards an Understanding of Mesocestoides vogae Fatty Acid Binding Proteins’ Roles

et al. 2014

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Two fatty acid binding proteins, MvFABPa and MvFABPb were identified in the parasite Mesocestoides vogae (Platyhelmithes, Cestoda). Fatty acid binding proteins are small intracellular proteins whose members exhibit great diversity. Proteins of this family have been identified in many organisms, of which Platyhelminthes are among the most primitive. These proteins have particular relevance in flatworms since de novo synthesis of fatty acids is absent. Fatty acids should be captured from the media needing an efficient transport system to uptake and distribute these molecules. While HLBPs could be involved in the shuttle of fatty acids to the surrounding host tissues and convey them into the parasite, FABPs could be responsible for the intracellular trafficking. In an effort to understand the role of MvFABPs in fatty acid transport of M. vogae larvae, we analysed the intracellular localization of both MvFABPs and the co-localization with in vivo uptake of fatty acid analogue BODIPY FL C16. Immunohistochemical studies on larvae sections using specific antibodies, showed a diffuse cytoplasmic distribution of each protein with some expression in nuclei and mitochondria. MvFABPs distribution was confirmed by mass spectrometry identification from 2D-electrophoresis of larvae subcellular fractions. This work is the first report showing intracellular distribution of MvFABPs as well as the co-localization of these proteins with the BODIPY FL C16 incorporated from the media. Our results suggest that fatty acid binding proteins could target fatty acids to cellular compartments including nuclei. In this sense, M. vogae FABPs could participate in several cellular processes fulfilling most of the functions attributed to vertebrate’s counterparts.

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Mesocestoides corti (syn. vogae, cestoda): Characterization of genes encoding cysteine-rich secreted proteins (CRISP)

Cited by 9 publications

References 31 publications

Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum

Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum

Transcriptomic Insights into the Diversity and Evolution of Myxozoa (Cnidaria, Endocnidozoa) Toxin-like Proteins

Towards an Understanding of Mesocestoides vogae Fatty Acid Binding Proteins’ Roles

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