Cloning and analysis of a Trichinella pseudospiralis muscle larva secreted serine protease gene

Cwiklinski, K; Meskill, D; Robinson, MW; Pozio, E; Appleton, JA; Connolly, B

Cloning and analysis of a Trichinella pseudospiralis muscle larva secreted serine protease gene

Cwiklinski, K Meskill, D Robinson, MW

Pozio, E Appleton, JA Connolly, B

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Publication Type:: Journal Article
Citation:: Veterinary Parasitology, 2009, 159 (3-4), pp. 268 - 271
Issue Date:: 2009-02-23

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Field	Value	Language
dc.contributor.author	Cwiklinski, K	en_US
dc.contributor.author	Meskill, D	en_US
dc.contributor.author	Robinson, MW https://orcid.org/0000-0001-7191-0034	en_US
dc.contributor.author	Pozio, E	en_US
dc.contributor.author	Appleton, JA	en_US
dc.contributor.author	Connolly, B	en_US
dc.date.issued	2009-02-23	en_US
dc.identifier.citation	Veterinary Parasitology, 2009, 159 (3-4), pp. 268 - 271	en_US
dc.identifier.issn	0304-4017	en_US
dc.identifier.uri	http://hdl.handle.net/10453/14895
dc.description.abstract	Nematode parasites of the genus Trichinella are intracellular and distinct life cycle stages invade intestinal epithelial and skeletal muscle cells. Within the genus, Trichinella spiralis and Trichinella pseudospiralis exhibit species-specific differences with respect to host-parasite complex formation and host immune modulation. Parasite excretory-secretory (ES) proteins play important roles at the host-parasite interface and are thought to underpin these differences in biology. Serine proteases are among the most abundant group of T. spiralis ES proteins and multiple isoforms of the muscle larvae-specific TspSP-1 serine protease have been identified. Recently, a similar protein (TppSP-1) in T. pseudospiralis muscle larvae was identified. Here we report the cloning and characterisation of the full-length transcript of TppSP-1 and present comparative data between TspSP-1 and TppSP-1. © 2008 Elsevier B.V. All rights reserved.	en_US
dc.relation.ispartof	Veterinary Parasitology	en_US
dc.relation.isbasedon	10.1016/j.vetpar.2008.10.036	en_US
dc.subject.classification	Mycology & Parasitology	en_US
dc.subject.mesh	Muscle, Skeletal	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Mice	en_US
dc.subject.mesh	Trichinella	en_US
dc.subject.mesh	Cloning, Molecular	en_US
dc.subject.mesh	Gene Expression Regulation, Enzymologic	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Larva	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Serine Proteases	en_US
dc.title	Cloning and analysis of a Trichinella pseudospiralis muscle larva secreted serine protease gene	en_US
dc.type	Journal Article
utslib.citation.volume	3-4	en_US
utslib.citation.volume	159	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	0704 Fisheries Sciences	en_US
utslib.for	0707 Veterinary Sciences	en_US
dc.location.activity	Netherlands
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	3-4	en_US
pubs.publication-status	Published	en_US
pubs.volume	159	en_US

Abstract:

Nematode parasites of the genus Trichinella are intracellular and distinct life cycle stages invade intestinal epithelial and skeletal muscle cells. Within the genus, Trichinella spiralis and Trichinella pseudospiralis exhibit species-specific differences with respect to host-parasite complex formation and host immune modulation. Parasite excretory-secretory (ES) proteins play important roles at the host-parasite interface and are thought to underpin these differences in biology. Serine proteases are among the most abundant group of T. spiralis ES proteins and multiple isoforms of the muscle larvae-specific TspSP-1 serine protease have been identified. Recently, a similar protein (TppSP-1) in T. pseudospiralis muscle larvae was identified. Here we report the cloning and characterisation of the full-length transcript of TppSP-1 and present comparative data between TspSP-1 and TppSP-1. © 2008 Elsevier B.V. All rights reserved.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/14895