The kunitz domain protein BLI-5 plays a functionally conserved role in cuticle formation in a diverse range of nematodes

Stepek, G., McCormack, G. and Page, A. P. (2010) The kunitz domain protein BLI-5 plays a functionally conserved role in cuticle formation in a diverse range of nematodes. Molecular and Biochemical Parasitology, 169(1), pp. 1-11. (doi: 10.1016/j.molbiopara.2009.08.005)

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Publisher's URL: http://dx.doi.org/10.1016/j.molbiopara.2009.08.005

Abstract

The cuticle of parasitic nematodes performs many critical functions and is essential for proper development and for protection from the host immune response. The biosynthesis, assembly, modification and turnover of this exoskeleton have been most extensively studied in the free-living nematode, Caenorhabditis elegans, where it represents a complex multi-step process involving a whole suite of enzymes. The biosynthesis of the cuticle has an additional level of complexity, as many of the enzymes also require additional proteins to aid their activation and selective inhibition. Blister-5 (BLI-5) represents a protein with a kunitz-type serine protease interacting domain and is involved in cuticle collagen biosynthesis in C. elegans, through its interaction with subtilisin-like processing enzymes (such as BLI-4). Mutation of the bli-5 gene causes blistering of the collagenous adult cuticle. Homologues of BLI-5 have been identified in several parasitic species that span different nematode clades. In this study, we molecularly and biochemically characterize BLI-5 homologues from the clade V nematodes C. elegans and Haemonchus contortus and from the clade III filarial nematode Brugia malayi. The nematode BLI-5 orthologues possess a shared domain structure and perform similar in vitro and in vivo functions, performing important proteolytic enzyme functions. The results demonstrate that the bli-5 genes from these diverse parasitic nematodes are able to complement a C. elegansbli-5 mutant and thereby support the use of the C. elegans model system to examine gene function in the experimentally less-amenable parasitic species.

Item Type:Articles (Other)
Keywords:Collagen, cuticle, caenorhabditis elegans, haemonchus contortus, brugia malayi
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:McCormack, Ms Gillian and Page, Professor Tony and Stepek, Dr Gillian
Authors: Stepek, G., McCormack, G., and Page, A. P.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Molecular and Biochemical Parasitology
Journal Abbr.:Mol. biochem. parasitol.
Publisher:Elsevier BV
ISSN:0166-6851
ISSN (Online):1872-9428
Published Online:27 August 2009
Copyright Holders:Copyright © 2009 Elsevier
First Published:First published in Molecular and Biochemical Parasitology 169(1):1-11
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
229993The Molecular Enzymology of Collagen Assembly and Post-Translational Modification: a Nematode Model SystemAntony PageMedical Research Council (MRC)G117/476Infection Immunity and Inflammation Life Sciences