Comparative analysis of the excretory-secretory proteome of the muscle larva of Trichinella pseudospiralis and Trichinella spiralis

Robinson, MW; Greig, R; Beattie, KA; Lamont, DJ; Connolly, B

Comparative analysis of the excretory-secretory proteome of the muscle larva of Trichinella pseudospiralis and Trichinella spiralis

Robinson, MW

Greig, R Beattie, KA Lamont, DJ Connolly, B

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Publication Type:: Journal Article
Citation:: International Journal for Parasitology, 2007, 37 (2), pp. 139 - 148
Issue Date:: 2007-02-01

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Field	Value	Language
dc.contributor.author	Robinson, MW https://orcid.org/0000-0001-7191-0034	en_US
dc.contributor.author	Greig, R	en_US
dc.contributor.author	Beattie, KA	en_US
dc.contributor.author	Lamont, DJ	en_US
dc.contributor.author	Connolly, B	en_US
dc.date.available	2006-08-21	en_US
dc.date.issued	2007-02-01	en_US
dc.identifier.citation	International Journal for Parasitology, 2007, 37 (2), pp. 139 - 148	en_US
dc.identifier.issn	0020-7519	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8655
dc.description.abstract	The nematodes Trichinella spiralis and Trichinella pseudospiralis are both intracellular parasites of skeletal muscle cells and induce profound alterations in the host cell resulting in a re-alignment of muscle-specific gene expression. While T. spiralis induces the production of a collagen capsule surrounding the host-parasite complex, T. pseudospiralis exists in a non-encapsulated form and is also characterised by suppression of the host inflammatory response in the muscle. These observed differences between the two species are thought to be due to variation in the proteins excreted or secreted (ES proteins) by the muscle larva. In this study, we use a global proteomics approach to compare the ES protein profiles from both species and to identify individual T. pseudospiralis proteins that complement earlier studies with T. spiralis. Following two-dimensional gel electrophoresis, tandem mass spectrometry was used to identify the peptide spots. In many cases identification was aided by the determination of partial peptide sequence from selected mass ions. The T. pseudospiralis spots identified included the major secreted glycoproteins and the secreted 5′-nucleotidase. Furthermore, two major groups of T. spiralis-specific proteins and several T. pseudospiralis-specific proteins were identified. Our results demonstrate the value of proteomics as a tool for the identification of ES proteins that are differentially expressed between Trichinella species and as an aid to identifying key parasite proteins that are involved in the host-parasite interaction. The value of this approach will be further enhanced by data arising out the current T. spiralis genome sequencing project. © 2006 Australian Society for Parasitology Inc.	en_US
dc.relation.ispartof	International Journal for Parasitology	en_US
dc.relation.isbasedon	10.1016/j.ijpara.2006.08.007	en_US
dc.subject.classification	Mycology & Parasitology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Mice, Inbred ICR	en_US
dc.subject.mesh	Mice	en_US
dc.subject.mesh	Trichinella	en_US
dc.subject.mesh	Helminth Proteins	en_US
dc.subject.mesh	Proteome	en_US
dc.subject.mesh	Antigens, Helminth	en_US
dc.subject.mesh	Electrophoresis, Gel, Two-Dimensional	en_US
dc.subject.mesh	Species Specificity	en_US
dc.subject.mesh	Larva	en_US
dc.subject.mesh	Mass Spectrometry	en_US
dc.title	Comparative analysis of the excretory-secretory proteome of the muscle larva of Trichinella pseudospiralis and Trichinella spiralis	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.citation.volume	37	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	0608 Zoology	en_US
utslib.for	0707 Veterinary Sciences	en_US
dc.location.activity	England
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
utslib.copyright.status	closed_access
pubs.issue	2	en_US
pubs.publication-status	Published	en_US
pubs.volume	37	en_US

Abstract:

The nematodes Trichinella spiralis and Trichinella pseudospiralis are both intracellular parasites of skeletal muscle cells and induce profound alterations in the host cell resulting in a re-alignment of muscle-specific gene expression. While T. spiralis induces the production of a collagen capsule surrounding the host-parasite complex, T. pseudospiralis exists in a non-encapsulated form and is also characterised by suppression of the host inflammatory response in the muscle. These observed differences between the two species are thought to be due to variation in the proteins excreted or secreted (ES proteins) by the muscle larva. In this study, we use a global proteomics approach to compare the ES protein profiles from both species and to identify individual T. pseudospiralis proteins that complement earlier studies with T. spiralis. Following two-dimensional gel electrophoresis, tandem mass spectrometry was used to identify the peptide spots. In many cases identification was aided by the determination of partial peptide sequence from selected mass ions. The T. pseudospiralis spots identified included the major secreted glycoproteins and the secreted 5′-nucleotidase. Furthermore, two major groups of T. spiralis-specific proteins and several T. pseudospiralis-specific proteins were identified. Our results demonstrate the value of proteomics as a tool for the identification of ES proteins that are differentially expressed between Trichinella species and as an aid to identifying key parasite proteins that are involved in the host-parasite interaction. The value of this approach will be further enhanced by data arising out the current T. spiralis genome sequencing project. © 2006 Australian Society for Parasitology Inc.

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http://hdl.handle.net/10453/8655