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  Identification of candidate mimicry proteins involved in parasite-driven phenotypic changes

Hebert, F. O., Samonte, I., Phelps, L., Panchal, M., Grambauer, S., Barber, I., et al. (2015). Identification of candidate mimicry proteins involved in parasite-driven phenotypic changes. Parasites & Vectors, 8(225). doi:10.1186/s13071-015-0834-1.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-BCFC-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-83F1-9
Genre: Journal Article

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 Creators:
Hebert, Francois Olivier, Author
Samonte, Irene1, Author              
Phelps, Luke2, Author              
Panchal, Mahesh1, Author              
Grambauer, Stephan, Author
Barber, Iain, Author
Kalbe, Martin1, Author              
Landry, Christian R, Author
Aubin-Horth, Nadia, Author
Affiliations:
1Department Evolutionary Ecology, Max Planck Institute for Evolutionary Biology, Max Planck Society, ou_1445634              
2Research Group Parasitology, Department Evolutionary Ecology, Max Planck Institute for Evolutionary Biology, Max Planck Society, ou_1445643              

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Free keywords: Parasites, Schistocephalus solidus; Cestodes; Ecological genomics; Genomics/proteomics; Molecular mimicry; Host-parasite interactions; Wnt; RT-PCR
 Abstract: Background Endoparasites with complex life cycles are faced with several biological challenges, as they need to occupy various ecological niches throughout their development. Host phenotypes that increase the parasite’s transmission rate to the next host have been extensively described, but few mechanistic explanations have been proposed to describe their proximate causes. In this study we explore the possibility that host phenotypic changes are triggered by the production of mimicry proteins from the parasite by using an ecological model system consisting of the infection of the threespine stickleback ( Gasterosteus aculeatus ) by the cestode Schistocephalus solidus . Method Using RNA-seq data, we assembled 9,093 prot ein-coding genes from which ORFs were predicted to generate a reference proteome. Based on a previously published method, we built two complementary analysis pipelines to i) establish a general classification of protein similarity among various species (pipeline A) and ii) identify candidate mimicry proteins showing specific host-parasite similarities (pipeline B), a key feature underlying the possibility of molecular mimicry. Results Ninety-four tapeworm proteins showed high local sequence homology with stickleback proteins. Four of these candidates correspond to secreted or membrane proteins that could be produced by the parasite and eventually be rele ased in or be in contact with the host to modulate physiological pathways involved in various phenotypes (e.g. behaviors). One of these candidates belongs to the Wnt family, a large group of signaling molecules involved in cell-to-cell interactions and various developmental pathways. The three other candidates are involved in ion transport and post-translational protein modifications. We further confirmed that these four candidates are expressed in thre e different developmental stages of the cestode by RT-PCR, including the stages found in the host. Conclusion In this study, we identified mimicry candida te peptides from a behavior-altering cestode showing specific sequence similarity with host proteins. Despite their potential role in modulating host pathways that could lead to parasite-induced phenotypic changes and despite our confirmation that they are expressed in the developmental stage corresponding to the altered host behavior, further investigations will be needed to confirm their mechanistic role in the molecular cross-talk taking place between S. solidus and the threespine stickleback.

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Language(s): eng - English
 Dates: 2015-03-102015-03-292015-04-15
 Publication Status: Published online
 Pages: -
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 Rev. Method: -
 Identifiers: DOI: 10.1186/s13071-015-0834-1
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Title: Parasites & Vectors
Source Genre: Journal
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Publ. Info: London : BioMed Central
Pages: 28 S. Volume / Issue: 8 (225) Sequence Number: - Start / End Page: - Identifier: n.a.: http://pubman.mpdl.mpg.de/cone/journals/resource/1756-3305