The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodes

Stepek, G., McCormack, G., Birnie, A.J. and Page, A.P. (2011) The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodes. Parasitology, 138(2), pp. 237-248. (doi: 10.1017/S0031182010001113) (PMID:20800010)

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Nematodes represent one of the most abundant and species-rich groups of animals on the planet, with parasitic species causing chronic, debilitating infections in both livestock and humans worldwide. The prevalence and success of the nematodes is a direct consequence of the exceptionally protective properties of their cuticle. The synthesis of this cuticle is a complex multi-step process, which is repeated 4 times from hatchling to adult and has been investigated in detail in the free-living nematode, Caenorhabditis elegans. This process is known as moulting and involves numerous enzymes in the synthesis and degradation of the collagenous matrix. The nas-36 and nas-37 genes in C. elegans encode functionally conserved enzymes of the astacin metalloprotease family which, when mutated, result in a phenotype associated with the late-stage moulting defects, namely the inability to remove the preceding cuticle. Extensive genome searches in the gastrointestinal nematode of sheep, Haemonchus contortus, and in the filarial nematode of humans, Brugia malayi, identified NAS-36 but not NAS-37 homologues. Significantly, the nas-36 gene from B. malayi could successfully complement the moult defects associated with C. elegans nas-36, nas-37 and nas-36/nas-37 double mutants, suggesting a conserved function for NAS-36 between these diverse nematode species. This conservation between species was further indicated when the recombinant enzymes demonstrated a similar range of inhibitable metalloprotease activities.

Item Type:Articles
Keywords:Haemonchus contortus, Brugia malayi, Caenorhabditis elegans, astacin metalloprotease, moulting, cuticle
Glasgow Author(s) Enlighten ID:Stepek, Dr Gillian and McCormack, Ms Gillian and Page, Professor Tony
Authors: Stepek, G., McCormack, G., Birnie, A.J., and Page, A.P.
Subjects:Q Science > QR Microbiology
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Parasitology
Published Online:27 August 2010
Copyright Holders:Copyright © 2010 Cambridge University Press
First Published:First published in Parasitology 138(2):237-248
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
403961Moulting and hatching in nematodes - the role of astacin metalloproteases as potential anti-nematode targetsAntony PageBiotechnology and Biological Sciences Research Council (BBSRC)BB/D000661/1Infection Immunity and Inflammation Life Sciences