Helminth pathogen cathepsin proteases: it's a family affair

Robinson, MW; Dalton, JP; Donnelly, S

Helminth pathogen cathepsin proteases: it's a family affair

Robinson, MW

Dalton, JP Donnelly, S

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Publication Type:: Journal Article
Citation:: Trends in Biochemical Sciences, 2008, 33 (12), pp. 601 - 608
Issue Date:: 2008-12-01

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Field	Value	Language
dc.contributor.author	Robinson, MW https://orcid.org/0000-0001-7191-0034	en_US
dc.contributor.author	Dalton, JP	en_US
dc.contributor.author	Donnelly, S https://orcid.org/0000-0003-2005-3698	en_US
dc.date.available	2008-09-04	en_US
dc.date.issued	2008-12-01	en_US
dc.identifier.citation	Trends in Biochemical Sciences, 2008, 33 (12), pp. 601 - 608	en_US
dc.identifier.issn	0968-0004	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8824
dc.description.abstract	Helminth pathogens express papain-like cysteine peptidases, termed cathepsins, which have important roles in virulence, including host entry, tissue migration and the suppression of host immune responses. The liver fluke Fasciola hepatica, an emerging human pathogen, expresses the largest cathepsin L cysteine protease family yet described. Recent phylogenetic, biochemical and structural studies indicate that this family contains five separate clades, which exhibit overlapping but distinct substrate specificities created by a process of gene duplication followed by subtle residue divergence within the protease active site. The developmentally regulated expression of these proteases correlates with the passage of the parasite through host tissues and its encounters with different host macromolecules. © 2008 Elsevier Ltd. All rights reserved.	en_US
dc.relation.ispartof	Trends in Biochemical Sciences	en_US
dc.relation.isbasedon	10.1016/j.tibs.2008.09.001	en_US
dc.subject.classification	Developmental Biology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Helminths	en_US
dc.subject.mesh	Fasciola hepatica	en_US
dc.subject.mesh	Cathepsins	en_US
dc.subject.mesh	Cysteine Endopeptidases	en_US
dc.subject.mesh	Helminth Proteins	en_US
dc.subject.mesh	Sequence Alignment	en_US
dc.subject.mesh	Phylogeny	en_US
dc.subject.mesh	Gene Expression Regulation, Developmental	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Substrate Specificity	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Host-Parasite Interactions	en_US
dc.title	Helminth pathogen cathepsin proteases: it's a family affair	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.citation.volume	33	en_US
utslib.for	0707 Veterinary Sciences	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access
pubs.issue	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	33	en_US

Abstract:

Helminth pathogens express papain-like cysteine peptidases, termed cathepsins, which have important roles in virulence, including host entry, tissue migration and the suppression of host immune responses. The liver fluke Fasciola hepatica, an emerging human pathogen, expresses the largest cathepsin L cysteine protease family yet described. Recent phylogenetic, biochemical and structural studies indicate that this family contains five separate clades, which exhibit overlapping but distinct substrate specificities created by a process of gene duplication followed by subtle residue divergence within the protease active site. The developmentally regulated expression of these proteases correlates with the passage of the parasite through host tissues and its encounters with different host macromolecules. © 2008 Elsevier Ltd. All rights reserved.

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http://hdl.handle.net/10453/8824