Excretory/secretory proteome of the adult stage of Echinostoma caproni

Sotillo, Javier; Valero, M. Luz; Pino, Manuel M. Sánchez del; Fried, Bernard; Esteban, J. Guillermo; Marcilla, Antonio; Toledo, Rafael

doi:10.1007/s00436-010-1923-x

Cited by 38 publications

(37 citation statements)

References 45 publications

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“…Although actin is a cytoskeletal protein, it has been detected in the ESP of different helminths such as Echinostoma caproni or Angiostrongylus cantonensis (54,55). Recently, parasitic trematodes were shown to secrete extracellular microvesicles that resembled mammalian exosomes (51), and accounts for the secretion of some proteins that lack a signal peptide.…”

Section: Discussionmentioning

confidence: 99%

Secreted Proteomes of Different Developmental Stages of the Gastrointestinal Nematode Nippostrongylus brasiliensis

Sotillo

Sánchez-Flores

Cantacessi

et al. 2014

Molecular & Cellular Proteomics

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ʈʈHookworms infect more than 700 million people worldwide and cause more morbidity than most other human parasitic infections. Nippostrongylus brasiliensis (the rat hookworm) has been used as an experimental model for human hookworm because of its similar life cycle and ease of maintenance in laboratory rodents. Adult N. brasiliensis, like the human hookworm, lives in the intestine of the host and releases excretory/secretory products (ESP), which represent the major host-parasite interface. We performed a comparative proteomic analysis of infective larval (

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Section: Discussionmentioning

confidence: 99%

Secreted Proteomes of Different Developmental Stages of the Gastrointestinal Nematode Nippostrongylus brasiliensis

Sotillo

Sánchez-Flores

Cantacessi

et al. 2014

Molecular & Cellular Proteomics

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“…We recently showed that significant percentage of proteins identified in MVs during malaria infection belong to classical and alternative complement pathway, components of cytoskeleton, glycolysis and lipid transport (Mantel et al, 2013). Metabolic enzymes related to glycolysis constitute the largest protein family in excretory/secretory proteome of helminth E.caproni (Sotillo et al, 2010). Some glycolytic enzymes in parasitic MVs have separate function that make them important for parasite survival and dissemination (for example, binding of plasminogen for enolase in Leishmania ) (Chandra et al, 2010).…”

Section: Microvesicle Proteomicsmentioning

confidence: 99%

Microvesicles and intercellular communication in the context of parasitism

Barteneva¹,

Maltsev²,

Vorobjev³

2013

Front. Cell. Infect. Microbiol.

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There is a rapidly growing body of evidence that production of microvesicles (MVs) is a universal feature of cellular life. MVs can incorporate microRNA (miRNA), mRNA, mtDNA, DNA and retrotransposons, camouflage viruses/viral components from immune surveillance, and transfer cargo between cells. These properties make MVs an essential player in intercellular communication. Increasing evidence supports the notion that MVs can also act as long-distance vehicles for RNA molecules and participate in metabolic synchronization and reprogramming eukaryotic cells including stem and germinal cells. MV ability to carry on DNA and their general distribution makes them attractive candidates for horizontal gene transfer, particularly between multi-cellular organisms and their parasites; this suggests important implications for the co-evolution of parasites and their hosts. In this review, we provide current understanding of the roles played by MVs in intracellular pathogens and parasitic infections. We also discuss the possible role of MVs in co-infection and host shifting.

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“…Proteins can be secreted from cells via the classical and non-classical pathways [2,3,8,9,23,30,31]. In the classical pathway, proteins that contain a specific N-terminal signal sequence are translocated into the ER, transported to the Golgi and then secreted by secretory vesicles [30,32,33].…”

Section: Introductionmentioning

confidence: 99%

Glucose induces rapid changes in the secretome of Saccharomyces cerevisiae

2014

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BackgroundProtein secretion is a fundamental process in all living cells. Proteins can either be secreted via the classical or non-classical pathways. In Saccharomyces cerevisiae, gluconeogenic enzymes are in the extracellular fraction/periplasm when cells are grown in media containing low glucose. Following a transfer of cells to high glucose media, their levels in the extracellular fraction are reduced rapidly. We hypothesized that changes in the secretome were not restricted to gluconeogenic enzymes. The goal of the current study was to use a proteomic approach to identify extracellular proteins whose levels changed when cells were transferred from low to high glucose media.ResultsWe performed two iTRAQ experiments and identified 347 proteins that were present in the extracellular fraction including metabolic enzymes, proteins involved in oxidative stress, protein folding, and proteins with unknown functions. Most of these proteins did not contain typical ER-Golgi signal sequences. Moreover, levels of many of these proteins decreased upon a transfer of cells from media containing low to high glucose media. Using an extraction procedure and Western blotting, we confirmed that the metabolic enzymes (glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, glucose-6-phosphate dehydrogenase, pyruvate decarboxylase), proteins involved in oxidative stress (superoxide dismutase and thioredoxin), and heat shock proteins (Ssa1p, Hsc82p, and Hsp104p) were in the extracellular fraction during growth in low glucose and that the levels of these extracellular proteins were reduced when cells were transferred to media containing high glucose. These proteins were associated with membranes in vesicle-enriched fraction. We also showed that small vesicles were present in the extracellular fraction in cells grown in low glucose. Following a transfer from low to high glucose media for 30 minutes, 98% of these vesicles disappeared from the extracellular fraction.ConclusionsOur data indicate that transferring cells from low to high glucose media induces a rapid decline in levels of a large number of extracellular proteins and the disappearance of small vesicles from the extracellular fraction. Therefore, we conclude that the secretome undergoes dynamic changes during transition from glucose-deficient to glucose-rich media. Most of these extracellular proteins do not contain typical ER signal sequences, suggesting that they are secreted via the non-classical pathway.

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Excretory/secretory proteome of the adult stage of Echinostoma caproni

Cited by 38 publications

References 45 publications

Secreted Proteomes of Different Developmental Stages of the Gastrointestinal Nematode Nippostrongylus brasiliensis

Secreted Proteomes of Different Developmental Stages of the Gastrointestinal Nematode Nippostrongylus brasiliensis

Microvesicles and intercellular communication in the context of parasitism

Glucose induces rapid changes in the secretome of Saccharomyces cerevisiae

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