Stepek, G., McCormack, G. and Page, A. P. (2010) Collagen processing and cuticle formation is catalysed by the astacin metalloprotease DPY-31 in free-living and parasitic nematodes. International Journal for Parasitology, 40(5), pp. 533-542. (doi: 10.1016/j.ijpara.2009.10.007) (PMID:19883650)
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Publisher's URL: http://dx.doi.org/10.1016/j.ijpara.2009.10.007
Abstract
The exoskeleton or cuticle performs many key roles in the development and survival of all nematodes. This structure is predominantly collagenous in nature and requires numerous enzymes to properly fold, modify, process and cross-link these essential structural proteins. The cuticle structure and its collagen components are conserved throughout the nematode phylum but differ from the collagenous matrices found in vertebrates. This structure, its formation and the enzymology of nematode cuticle collagen biogenesis have been elucidated in the free-living nematode Caenorhabditis elegans. The dpy-31 gene in C. elegans encodes a procollagen C-terminal processing enzyme of the astacin metalloprotease or bone morphogenetic protein class that, when mutated, results in a temperature-sensitive lethal phenotype associated with cuticle defects. In this study, orthologues of this essential gene have been identified in the phylogenetically diverse parasitic nematodes Haemonchus contortus and Brugia malayi. The DPY-31 protein is expressed in the gut and secretory system of C. elegans, a location also confirmed when a B. malayi transcriptional dpy-31 promoter-reporter gene fusion was expressed in C. elegans. Functional conservation between the nematode enzymes was supported by the fact that heterologous expression of the H. contortus dpy-31 orthologue in a C. elegans dpy-31 mutant resulted in the full rescue of the mutant body form. This interspecies conservation was further established when the recombinant nematode enzymes were found to have a similar range of inhibitable protease activities. In addition, the recombinant DPY-31 enzymes from both H. contortus and B. malayi were shown to efficiently process the C. elegans cuticle collagen SQT-3 at the correct C-terminal procollagen processing site.
| Item Type: | Articles |
|---|---|
| Keywords: | Caenorhabditis elegans, haemonchus contortus, brugia malayi, astacin metalloprotease, BMP, development, cuticle |
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Page, Professor Tony and McCormack, Ms Gillian and Stepek, Dr Gillian |
| Authors: | Stepek, G., McCormack, G., and Page, A. P. |
| Subjects: | Q Science > QL Zoology Q Science > QH Natural history > QH345 Biochemistry |
| College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity |
| Journal Name: | International Journal for Parasitology |
| Journal Abbr.: | Int. j. parasitol. |
| Publisher: | Elsevier on behalf of the Australian Society for Parasitology |
| ISSN: | 0020-7519 |
| ISSN (Online): | 1879-0135 |
| Published Online: | 31 October 2009 |
| Copyright Holders: | Copyright © 2009 Australian Society for Parasitology |
| First Published: | First published in International Journal for Parasitology 40(5):533-542 |
| Publisher Policy: | Reproduced in accordance with the copyright policy of the publisher |
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