Insights into blood feeding by schistosomes from a proteomic analysis of worm vomitus

Hall, Stephanie L.; Braschi, Bryony; Truscott, Martha; Mathieson, William; Cesari, Italo M.; Wilson, R. A.

doi:10.1016/j.molbiopara.2011.05.002

Cited by 77 publications

(131 citation statements)

References 53 publications

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“…During a proteomic analysis of worm vomitus, the authors detected a schistosome serpin identified with gene Smp_090080 corresponding to Smpi56/C4QLC6. Within this environment, the protein was hypothesized to function as an inhibitor of coagulation of ingested blood (Hall et al, 2011). Indeed, immunofluorescence studies of Sj serpin using sliced S. japonicum samples revealed distinct staining of intestinal epithelia in addition to the tegument (Yan et al, 2005) and, retrospectively, our previous studies on ShSPI using intact parasites are compatible with a similar distribution in S. haematobium (Blanton et al, 1994).…”

Section: Biological Role Of Shspisupporting

confidence: 61%

Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain

Granzin¹,

Huang²,

Topbaş³

et al. 2012

Acta Crystallogr D Biol Cryst

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Parasitic organisms are constantly challenged by the defence mechanisms of their respective hosts, which often depend on serine protease activities. Consequently, protease inhibitors such as those belonging to the serpin superfamily have emerged as protective elements that support the survival of the parasites. This report describes the crystal structure of ShSPI, a serpin from the trematode Schistosoma haematobium. The protein is exposed on the surface of invading cercaria as well as of adult worms, suggesting its involvement in the parasite–host interaction. While generally conforming to the well established serpin fold, the structure reveals several distinctive features, mostly concerning the helical subdomain of the protein. It is proposed that these peculiarities are related to the unique biological properties of a small serpin subfamily which is conserved among pathogenic schistosomes.

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Section: Biological Role Of Shspisupporting

confidence: 61%

Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain

Granzin¹,

Huang²,

Topbaş³

et al. 2012

Acta Crystallogr D Biol Cryst

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“…hepatica (66). Indeed, the same proteins were also identified in vomitus from both of the latter trematodes and S. mansoni (66,78).…”

Section: Discussionmentioning

confidence: 80%

“…Recent proteomic studies of S. mansoni (blood fluke) and Fa. hepatica vomitus also identified a number of lysosomal proteins as enzymes putatively involved in digestive processes (66,78). In S. mansoni, this observation led to the hypothesis that lysosomal proteases might be actively secreted into the gut lumen, the pH of which facilitates the activity of these proteins, in order to SC, number of unique peptides assigned to the protein; CO, percent cover; LO, putative subcellular localization of the protein; TM, number of transmembrane domains.…”

Section: Discussionmentioning

confidence: 99%

“…The presence of a signal peptide (SP) or an N-linked glycosylation site (N) is denoted by "ϩ"; the presence of the protein in the ES of adult Fasciola hepatica (Fh), Clonorchis sinensis (Cs), or Opisthorchis viverrini (Ov) is also denoted by "ϩ." enable the digestion of plasma components as well as hemoglobin (78). A legumain, a pro-X carboxylpeptidase, a betaglucosidase, several isoforms of ferritin, and the NiemannPick C2 protein were also identified here as constituents of the ES products from F. magna.…”

Section: Discussionmentioning

confidence: 99%

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A Deep Exploration of the Transcriptome and “Excretory/Secretory” Proteome of Adult Fascioloides magna

Cantacessi

Mulvenna

Young

et al. 2012

Molecular & Cellular Proteomics

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Parasitic liver flukes of the family Fasciolidae are responsible for major socioeconomic losses worldwide. However, at present, knowledge of the fundamental molecular biology of these organisms is scant. Here, we characterize, for the first time, the transcriptome and secreted proteome of the adult stage of the "giant liver fluke," Fascioloides magna, using Illumina sequencing technology and one-dimensional SDS-PAGE and OFFGEL protein electrophoresis, respectively. A total of ϳ54,000,000 reads were generated and assembled into ϳ39,000 contiguous sequences (contigs); ϳ20,000 peptides were predicted and classified based on homology searches, protein motifs, gene ontology, and biological pathway mapping. From the predicted proteome, 48.1% of proteins could be assigned to 384 biological pathway terms, including "spliceosome," "RNA transport," and "endocytosis." Putative proteins involved in amino acid degradation were most abundant. Of the 835 secreted proteins predicted from the transcriptome of F. magna, 80 were identified in the excretory/secretory products from this parasite. Highly represented were antioxidant proteins, followed by peptidases (particularly cathepsins) and proteins involved in carbohydrate metabolism. The integration of transcriptomic and proteomic datasets generated herein sets the scene for future studies aimed at exploring the potential role(s) that molecules might play at the hostparasite interface and for establishing novel strategies for the treatment or control of parasitic fluke infections. Molecular & Cellular

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“…This result indicates that SmATPDase1 is not released by schistosomes even after prolonged incubation, and that if SmATPDase2 is released, it is not capable of degrading ATP under the conditions used. Further evidence that SmATPDase2 is not secreted by schistosomes comes from proteomic analysis of material released by schistosomes following 96 h in culture; SmATPDase2 is not among the many proteins detected [28]. In addition, protein sequence analysis reveals that, unlike SmATPDase1, SmATPDase2 is devoid of a predicted canonical signal peptide (and any transmembrane domain) [18].…”

Section: Discussionmentioning

confidence: 99%

Schistosome apyrase SmATPDase1, but not SmATPDase2, hydrolyses exogenous ATP and ADP

Da’dara¹,

Bhardwaj²,

Skelly³

2014

Purinergic Signalling

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Schistosomes are parasitic worms that can live in the bloodstream of their vertebrate hosts for many years. It has been proposed that the worms impinge on host purinergic signalling by degrading proinflammatory molecules like ATP as well as prothrombotic mediators like ADP. This capability may help explain the apparent refractoriness of the worms to both immune elimination and thrombus formation. Three distinct ectoenzymes, expressed at the host-exposed surface of the worm's tegument, are proposed to be involved in the catabolism of ATP and ADP. These are alkaline phosphatase (SmAP), phosphodiesterase (SmNPP-5), and ATP diphosphohydrolase (SmATPDase1). It has recently been shown that only one of these enzymes-SmATPDase1-actually degrades exogenous ATP and ADP. However, a second ATP diphosphohydrolase homolog (SmATPDase2) is located in the tegument and has been reported to be released by the worms. It is possible that this enzyme too participates in the cleavage of exogenous nucleotide tri-and di-phosphates. To test this hypothesis, we employed RNA interference (RNAi) to suppress the expression of the schistosome SmATPDase1 and SmATPDase2 genes. We find that only SmATPDase1-suppressed parasites are significantly impaired in their ability to degrade exogenously added ATP or ADP. Suppression of SmATPDase2 does not appreciably affect the worms' ability to catabolize ATP or ADP. Furthermore, we detect no evidence for the secretion or release of an ATP-hydrolyzing activity by cultured parasites. The results confirm the role of tegumental SmATPDase1, but not SmADTPDase2, in the degradation of the exogenous proinflammatory and prothrombotic nucleotides ATP and ADP by live intravascular stages of the parasite.

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Insights into blood feeding by schistosomes from a proteomic analysis of worm vomitus

Cited by 77 publications

References 53 publications

Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain

Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain

A Deep Exploration of the Transcriptome and “Excretory/Secretory” Proteome of Adult Fascioloides magna

Schistosome apyrase SmATPDase1, but not SmATPDase2, hydrolyses exogenous ATP and ADP

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