Enzymology of the nematode cuticle: a potential drug target?

Page, A. P. , Stepek, G., Winter, A. D. and Pertab, D. (2014) Enzymology of the nematode cuticle: a potential drug target? International Journal for Parasitology: Drugs and Drug Resistance, 4(2), pp. 133-141. (doi: 10.1016/j.ijpddr.2014.05.003) (PMID:25057463) (PMCID:PMC4095051)

95064.pdf - Published Version
Available under License Creative Commons Attribution Non-commercial No Derivatives.



All nematodes possess an external structure known as the cuticle, which is crucial for their development and survival. This structure is composed primarily of collagen, which is secreted from the underlying hypodermal cells. Extensive studies using the free-living nematode <i>Caenorhabditis elegans</i> demonstrate that formation of the cuticle requires the activity of an extensive range of enzymes. Enzymes are required both pre-secretion, for synthesis of component proteins such as collagen, and post-secretion, for removal of the previous developmental stage cuticle, in a process known as moulting or exsheathment. The excretion/secretion products of numerous parasitic nematodes contain metallo-, serine and cysteine proteases, and these proteases are conserved across the nematode phylum and many are involved in the moulting/exsheathment process. This review highlights the enzymes required for cuticle formation, with a focus on the post-secretion moulting events. Where orthologues of the <i>C. elegans</i> enzymes have been identified in parasitic nematodes these may represent novel candidate targets for future drug/vaccine development.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Pertab, Mr David and Stepek, Dr Gillian and Winter, Dr Alan and Page, Professor Tony
Authors: Page, A. P., Stepek, G., Winter, A. D., and Pertab, D.
College/School:College of Medical Veterinary and Life Sciences > School of Biodiversity, One Health & Veterinary Medicine
Journal Name:International Journal for Parasitology: Drugs and Drug Resistance
ISSN (Online):2211-3207
Copyright Holders:Copyright © 2014 The Authors
First Published:First published in International Journal for Parasitology: Drugs and Drug Resistance 4(2):133-141
Publisher Policy:Reproduced under a Creative Commons License

University Staff: Request a correction | Enlighten Editors: Update this record

Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
543261The matrix associated astacin enzymes; novel targets in the control of key GI nematodes of ruminants.Antony PageBiotechnology and Biological Sciences Research Council (BBSRC)BB/I011218/1III - PARASITOLOGY