The cathepsin-like cysteine peptidases of trematodes of the genus Fasciola.

Cathepsin Cysteine peptidase Enzymes Fasciola Food-borne Genomics Helminths Phylogenetics Protein structure Proteinase Proteomics Transcriptomics Trematode Trematodes

Journal

Advances in parasitology
ISSN: 2163-6079
Titre abrégé: Adv Parasitol
Pays: England
ID NLM: 0370435

Informations de publication

Date de publication:
2019
Historique:
entrez: 30 4 2019
pubmed: 30 4 2019
medline: 14 1 2020
Statut: ppublish

Résumé

Fasciolosis caused by trematode parasites of the genus Fasciola is a global disease of livestock, particularly cattle, sheep, water buffalo and goats. It is also a major human zoonosis with reports suggesting that 2.4-17 million people are infected worldwide, and 91.1 million people currently living at risk of infection. A unique feature of these worms is their reliance on a family of developmentally-regulated papain-like cysteine peptidases, termed cathepsins. These proteolytic enzymes play central roles in virulence, infection, tissue migration and modulation of host innate and adaptive immune responses. The availability of a Fasciola hepatica genome, and the exploitation of transcriptomic and proteomic technologies to probe parasite growth and development, has enlightened our understanding of the cathepsin-like cysteine peptidases. Here, we clarify the structure of the cathepsin-like cysteine peptidase families and, in this context, review the phylogenetics, structure, biochemistry and function of these enzymes in the host-parasite relationship.

Identifiants

pubmed: 31030768
pii: S0065-308X(19)30001-6
doi: 10.1016/bs.apar.2019.01.001
pii:
doi:

Substances chimiques

Peptide Hydrolases EC 3.4.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

113-164

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L019612/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N017757/1
Pays : United Kingdom

Informations de copyright

© 2019 Elsevier Ltd. All rights reserved.

Auteurs

Krystyna Cwiklinski (K)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.

Sheila Donnelly (S)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom; The School of Life Sciences, University of Technology Sydney (UTS), Ultimo, Sydney, NSW, Australia.

Orla Drysdale (O)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.

Heather Jewhurst (H)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.

David Smith (D)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.

Carolina De Marco Verissimo (C)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.

Izanara C Pritsch (IC)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom; Department of Basic Pathology, Federal University of Parana, Curitiba, Brazil.

Sandra O'Neill (S)

School of Biotechnology, Dublin City University, Dublin, Republic of Ireland.

John P Dalton (JP)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.

Mark W Robinson (MW)

School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom. Electronic address: mark.robinson@qub.ac.uk.

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Classifications MeSH