Lipid binding proteins from parasitic platyhelminthes

Alvite, Gabriela; Esteves, Adriana

doi:10.3389/fphys.2012.00363

Cited by 17 publications

(17 citation statements)

References 51 publications

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“…Parasitic helminths do not synthesise fatty acids and instead acquire lipids and fatty acids from host-tissues, -fluids and/or intestinal content [ 16 ]. Indeed, many of the proteins within the excretory/secretory products of helminths include lipid-binding proteins for the appropriation of host-derived lipids [ 17 , 18 , 19 ]. Importantly, helminths do not metabolise fatty acids for energy production, rather, host-derived lipids are used in the biosynthesis of cell membranes or egg production [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

Fluorescent Labeling of Helminth Extracellular Vesicles Using an In Vivo Whole Organism Approach

et al. 2020

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In the last two decades, extracellular vesicles (EVs) from the three domains of life, Archaea, Bacteria and Eukaryotes, have gained increasing scientific attention. As such, the role of EVs in host-pathogen communication and immune modulation are being intensely investigated. Pivotal to EV research is the determination of how and where EVs are taken up by recipient cells and organs in vivo, which requires suitable tracking strategies including labelling. Labelling of EVs is often performed post-isolation which increases risks of non-specific labelling and the introduction of labelling artefacts. Here we exploited the inability of helminths to de novo synthesise fatty acids to enable labelling of EVs by whole organism uptake of fluorescent lipid analogues and the subsequent incorporation in EVs. We showed uptake of 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (DOPE-Rho) in Anisakis spp. and Trichuris suis larvae. EVs isolated from the supernatant of Anisakis spp. labelled with DOPE-Rho were characterised to assess the effects of labelling on size, structure and fluorescence of EVs. Fluorescent EVs were successfully taken up by the human macrophage cell line THP-1. This study, therefore, presents a novel staining method that can be utilized by the EV field in parasitology and potentially across multiple species.

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Section: Introductionmentioning

confidence: 99%

Fluorescent Labeling of Helminth Extracellular Vesicles Using an In Vivo Whole Organism Approach

et al. 2020

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“…In contrast, these taeniids have great capability to uptake nutrients; cysticerci absorb and consume large quantities of glucose through transporters TGTP1 and TGTP2 and store the excess as glycogen [5]. A similar phenomenon occurs with the acquisition of fatty acids and cholesterol from the host environment [6,7]. Amino acid absorption in T. crassiceps was reported several decades ago, through the proposal of three mechanisms specific for neutral, basic, and acidic amino acids [8,9].…”

Section: Introductionmentioning

confidence: 99%

Fate of uptaken host proteins in Taenia solium and Taenia crassiceps cysticerci

et al. 2018

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During the study of host-parasite relationships in taeniid parasite diseases, including cysticercosis and hydatidosis, reports have described the presence of host proteins in the cyst fluid and tissue of metacestodes. However, the fate or role of host elements inside the parasite remains barely explored. After the publication of genomes of four cestode species, it became clear that these organisms possess a limited biosynthetic capability. The initial goal of the present study was to determine if uptaken host proteins could be a source of essential amino acids for cysticerci. To track the utilization of uptaken proteins, we added metabolically labeled IgG-H and GFP-H to the culture medium of cysticerci. Incorporation of labeled amino acid was evaluated by fluorography in cysticerci extracts. Our results showed that the use of uptaken proteins by cysticerci as a source of amino acids appeared negligible. Exploring alternative fates for the host proteins, proteomic analysis of the protein matrix in calcareous corpuscles was carried out. Since does not contain calcareous corpuscles, proteomic analyses were performed in corpuscles of cysticerci. Our results demonstrated that host proteins represented approximately 70% of protein content in the calcareous corpuscles. The presence of the two major uptaken host proteins, namely albumin and IgG, was also demonstrated by Western blot in the matrix of corpuscles. Our findings strongly suggested that the uptake and disposal of host proteins involve calcareous corpuscles, expanding the physiological role of these mineral concretions to a far more important level than previously proposed.

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“…granulosus HF. AgB belongs to the group of hydrophobic ligand binding proteins (HLBPs), a cestode protein family whose members are known by their high abundance and immunogenicity, and by their oligomeric structure, comprising 7–10 kDa α-helix rich subunits [ 5 – 7 ]. AgB oligomers have been observed predominantly in the molecular mass range of 150–230 kDa, but aggregates with higher molecular masses have also been detected [ 8 , 9 ].…”

Section: Introductionmentioning

confidence: 99%

Antigen B from Echinococcus granulosus enters mammalian cells by endocytic pathways

Silva¹,

Cancela²,

Monteiro³

et al. 2018

PLoS Negl Trop Dis

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BackgroundCystic hydatid disease is a zoonosis caused by the larval stage (hydatid) of Echinococcus granulosus (Cestoda, Taeniidae). The hydatid develops in the viscera of intermediate host as a unilocular structure filled by the hydatid fluid, which contains parasitic excretory/secretory products. The lipoprotein Antigen B (AgB) is the major component of E. granulosus metacestode hydatid fluid. Functionally, AgB has been implicated in immunomodulation and lipid transport. However, the mechanisms underlying AgB functions are not completely known.Methodology/Principal findingsIn this study, we investigated AgB interactions with different mammalian cell types and the pathways involved in its internalization. AgB uptake was observed in four different cell lines, NIH-3T3, A549, J774 and RH. Inhibition of caveolae/raft-mediated endocytosis causes about 50 and 69% decrease in AgB internalization by RH and A549 cells, respectively. Interestingly, AgB colocalized with the raft endocytic marker, but also showed a partial colocalization with the clathrin endocytic marker. Finally, AgB colocalized with an endolysosomal tracker, providing evidence for a possible AgB destination after endocytosis.Conclusions/SignificanceThe results indicate that caveolae/raft-mediated endocytosis is the main route to AgB internalization, and that a clathrin-mediated entry may also occur at a lower frequency. A possible fate for AgB after endocytosis seems to be the endolysosomal system. Cellular internalization and further access to subcellular compartments could be a requirement for AgB functions as a lipid carrier and/or immunomodulatory molecule, contributing to create a more permissive microenvironment to metacestode development and survival.

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Lipid binding proteins from parasitic platyhelminthes

Cited by 17 publications

References 51 publications

Fluorescent Labeling of Helminth Extracellular Vesicles Using an In Vivo Whole Organism Approach

Fluorescent Labeling of Helminth Extracellular Vesicles Using an In Vivo Whole Organism Approach

Fate of uptaken host proteins in Taenia solium and Taenia crassiceps cysticerci

Antigen B from Echinococcus granulosus enters mammalian cells by endocytic pathways

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