Across intra-mammalian stages of the liver f luke Fasciola hepatica: a proteomic study

Abstract

Fasciola hepatica is the agent of fasciolosis, a foodborne zoonosis that affects livestock production and human health. Although flukicidal drugs are available, re-infection and expanding resistance to triclabendazole demand new control strategies. Understanding the molecular mechanisms underlying the complex interaction with the mammalian host could provide relevant clues, aiding the search for novel targets in diagnosis and control of fasciolosis. Parasite survival in the mammalian host is mediated by parasite compounds released during infection, known as excretory/secretory (E/S) products. E/S products are thought to protect parasites from host responses, allowing them to survive for a long period in the vertebrate host. This work provides in-depth proteomic analysis of F. hepatica intra-mammalian stages, and represents the largest number of proteins identified to date for this species. Functional classification revealed the presence of proteins involved in different biological processes, many of which represent original findings for this organism and are important for parasite survival within the host. These results could lead to a better comprehension of host-parasite relationships, and contribute to the development of drugs or vaccines against this parasite.

Genomes of Fasciola hepatica from the Americas Reveal Colonization with Neorickettsia Endobacteria Related to the Agents of Potomac Horse and Human Sennetsu Fevers

“…hepatica provide further support for the differential expression of these gene families [34], confirming our transcriptomic data (S3 Table). For example, within the cathepsin B family, members of 10 out of 13 clusters are detected by LC-MS/MS in ESPs; while 3 isoforms are exclusively expressed by adults, 2 are characteristic of juveniles (also detected by RNAseq in metacercariae), and 5 are expressed in both stages but clearly predominant in juveniles (Fig 1C).…”

“…Similarly, the cathepsins L-like of the trematodes (yellow arch) show a basal node more related to the mammalian enzymes and several independent amplifications in schistosomes, opistorchiids and Fasciola . Most known cathepsins variants are supported by expression data in different stages (red, green and blue bars), and proteomic data (yellow, green and blue dots) from a recent report [34]. Several putative novel variants are indicated, most of them not expressed at the stages analyzed.…”

Advances in Fasciola hepatica research using ‘omics’ technologies

“…Jefferies and colleagues (2000; improved this analysis using two-dimensional gel electrophoresis and subsequent characterisation and annotation of protein spots to identify a range of cathepsin L proteases, superoxide dismutase, peroxiredoxin, glutathione S-transferases and fatty acid binding proteins. This study formed the basis for further in-depth analyses of these protein families using modern proteomic techniques and phylogenetic tools to elucidate how these protein families have diverged and adapted (Chemale et al, 2006;Robinson et al, 2008;Marcilla et al, 2008;Morphew et al, 2011;Morphew et al, 2012;Morphew et al, 2013;Cwiklinski et al, 2015b;Morphew et al, 2016;Di Maggio et al, 2016). Furthermore, proteomic analysis of the proteins within the extracellular vesicles released within the secreted/excreted proteins has revealed that the 15K and 120K sub-populations of EVs released by F. hepatica vary in their protein cargo composition (Cwiklinski et al, 2015b).…”

In-depth proteomic characterization of Schistosoma haematobium: towards the development of new tools for elimination

“…Two GLIPR1 proteins (MS3_11039.1 and MS3_07294.1) were uniquely identified in the SEA dataset and were among the most abundant proteins based on spectrum counting. These proteins belong to the sperm-coating proteins/Tpx1/Ag5/PR-1/Sc7 (SCP/TAPS) family, and have been identified in other trematodes including Fasciola hepatica [80] as well as other helminths [81]. Although the exact function for these proteins is still unknown, this family of proteins is expanded in the genomes and secreted proteomes of clade IV and V nematodes [82–86] and is believed to play specific biological functions in the host including defence against host attack and determination of lifespan [87].…”