Dataset Information

Proteomic analysis of the secretome of Schistocephalus solidus LC-MS/MS

ABSTRACT: Schistocephalus solidus is a cestode parasite that is thought to manipulate the behaviour of its threespine stickleback host Gasterosteus aculeatus. It has been hypothesized that the worm could liberate in its external environment “manipulation factors” that would ultimately interfere with the host’s physiology and behaviour. The objective of this project is to describe the whole proteomic content of the proteome and of the secretome of a putative manipulative parasite, Schistocephalus solidus, with the aim to identify proteins that could be involved in the behavioural perturbations of the threespine stickleback.

INSTRUMENT(S): Bruker Daltonics instrument model

ORGANISM(S): Schistocephalus Solidus

TISSUE(S): Whole Body

SUBMITTER: Jenny Moon

LAB HEAD: Nadia Aubin-Horth

PROVIDER: PXD016844 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

The parasite Schistocephalus solidus secretes proteins with putative host manipulation functions.

Berger Chloé Suzanne CS Laroche Jérôme J Maaroufi Halim H Martin Hélène H Moon Kyung-Mee KM Landry Christian R CR Foster Leonard J LJ Aubin-Horth Nadia N

Parasites & vectors 20210828 1

<h4>Background</h4>Manipulative parasites are thought to liberate molecules in their external environment, acting as manipulation factors with biological functions implicated in their host's physiological and behavioural alterations. These manipulation factors are part of a complex mixture called the secretome. While the secretomes of various parasites have been described, there is very little data for a putative manipulative parasite. It is necessary to study the molecular interaction between a ...[more]

PMID: 34454597

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Project description:A highly recurrent, somatic L265P mutation in the TIR domain of the signaling adapter MYD88 constitutively activates NF-kB. It occurs in nearly all human patients with Waldenström’s macroglobulinemia (WM), a B cell malignancy caused by IgM-expressing cells. Here we introduced an inducible leucine to proline point mutation into the mouse Myd88 locus, at the orthologous position L252P. When the mutation was introduced early during B cell development, B cells developed normally. However, IgM-expressing plasma cells accumulated with age in spleen and bone, leading to more than 20-fold elevated serum IgM titers. When introduced into germinal center B cells in the context of an immunization, the Myd88L252P mutation caused prolonged persistence of antigen-specific serum IgM and elevated numbers of antigen-specific IgM plasma cells. Myd88L252P-expressing B cells switched normally, but plasma cells expressing other immunoglobulin isotypes did not increase in numbers, implying that IgM expression may be required for the observed cellular expansion. In order to test whether the Myd88L252P mutation can cause clonal expansions, we introduced it into a small fraction of CD19-positive B cells. In this scenario, five out of five mice developed monoclonal IgM serum paraproteins accompanied by an expansion of clonally related plasma cells that expressed mostly hypermutated VDJ regions. Taken together, our data suggest that the Myd88L252P mutation is sufficient to promote aberrant survival and expansion of IgM-expressing plasma cells which in turn can cause IgM monoclonal gammopathy of undetermined significance (MGUS), the premalignant condition that precedes WM. References: 1. Shevchenko A, Tomas H, Havli J, Olsen JV, Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc (2006) 1:2856–2860. doi:10.1038/nprot.2006.468, 2. Rappsilber J, Mann M, Ishihama Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc (2007) 2:1896–1906. doi:10.1038/nprot.2007.261, 3. Cox J, Neuhauser N, Michalski A, Scheltema RA, Olsen JV, Mann M. Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment. J Proteome Res (2011) 10:1794–1805. doi:10.1021/pr101065j, 4. Cox J, Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol (2008) 26:1367–1372. doi:10.1038/nbt.1511.

Dataset Information

Proteomic analysis of the secretome of Schistocephalus solidus LC-MS/MS

Publications

The parasite Schistocephalus solidus secretes proteins with putative host manipulation functions.

Similar Datasets

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