Dataset Information

Comparative proteomics of Adult Paragominus kellikotti excretion/secretion products released in vitro or present in the lung cyst nodule

ABSTRACT: The aims of this study were to study ESPs to improve understanding of parasite-host interactions and to support the discovery of novel diagnostic or therapeutic targets. We used tandem mass-spectrometry to characterize the secretome of adult P. kellicotti flukes and to compare ESPs released during in vitro culture with parasite cyst fluid proteins (CFPs) which correspond to ESPs released by adult flukes in vivo. We also compared these results to the global proteome of soluble, somatic protein (SSP) extracts of whole adult flukes.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Paragominus Kellikotti

SUBMITTER: Peter U. Fischer

PROVIDER: MSV000089589 | MassIVE | Thu Jun 02 16:05:00 BST 2022

SECONDARY ACCESSION(S): PXD034272

REPOSITORIES: MassIVE

ACCESS DATA

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Publications

Comparative proteomics of adult Paragonimus kellicotti excretion/secretion products released in vitro or present in the lung cyst nodule.

Di Maggio Lucia S LS Curtis Kurt C KC Erdmann-Gilmore Petra P Sprung Robert S W RSW Townsend R Reid RR Weil Gary J GJ Fischer Peter U PU

PLoS neglected tropical diseases 20220817 8

Paragonimus kellicotti is a zoonotic lung fluke infection, the agent of North American paragonimiasis, and an excellent model for other Paragonimus infections. The excretory/secretory proteins (ESP) released by parasites and presented at the parasite-host interface are frequently proposed to be useful targets for drugs and/or vaccines In vitro culture conditions may alter ESP compared to those produced in vivo. In order to investigate ESPs produced in vivo we took advantage of the fact that adul ...[more]

PMID: 35976975

Similar Datasets

Project description:Paragonimus kellicotti is a zoonotic lung fluke infection, the agent of North American paragonimiasis, and an excellent model for other Paragonimus infections. The excretory/secretory proteins (ESP) released by parasites and presented at the parasite-host interface are frequently proposed to be useful targets for drugs and/or vaccines In vitro culture conditions may alter ESP compared to those produced in vivo. In order to investigate ESPs produced in vivo we took advantage of the fact that adult P. kellicotti reproduce in the lungs of experimentally infected gerbils in tissue cysts. We performed a mass-spectrometric analysis of adult P. kellicotti soluble somatic protein (SSPs) extracts, excreted/secreted proteins (ESPs) produced by adult worms during in vitro culture, and lung cyst fluid proteins (CFPs) from experimentally infected gerbils. We identified 2,137 P. kellicotti proteins that were present in at least two of three biological replicates and supported by at least two peptides. Among those were 1,914 proteins found in SSP, 947 in ESP and 37 in CFP. In silico analysis predicted that only 141 of the total 2,137 proteins were secreted via classical or non-classical pathways. The most abundant functional categories in SSP were storage and oxidative metabolism. The most abundant categories in ESP were proteins related to metabolism and signal transduction. The 37 parasite-related proteins in CFP belonged to 11 functional categories. The largest groups were proteins with unknown function, cytoskeletal proteins and proteasome machinery. 29 of these 37 proteins were shared among all three sample types. To our knowledge, this is the first study that compares in vitro and in vivo ESP for any Paragonimus species. This study has provided new insights into ESPs of food-borne trematodes that are produced and released in vivo. Proteins released at the host-parasite interface may help the parasite evade host immunity and may represent new targets for novel treatments or diagnostic tests for paragonimiasis.