Biochemistry of the nematode cuticle: relevance to parasitic nematodes of livestock

Abstract

The cuticle of nematodes is a thin, flexible outer covering composed primarily of protein with trace amounts of lipid and carbohydrate. There has been considerable recent interest in the biochemistry, immunology and molecular biology of the cuticle of parasitic nematodes because of its role as an interface between parasite and host. The cuticle consists of: (1) collagen-like proteins that form the medial and basal layers; (2) non-collagen proteins that form the epicuticular and external cortical regions; (3) non-structural proteins associated with the external surface. The collagen-like proteins are solubilized by reducing agents, have molecular weights of 30–120 kDa and exhibit stage and species variations. Nematode collagen genes, however, code only for proteins with molecular weights of 30 kDa. The non-collagenous proteins, referred to as cuticlin, exhibit unusual chemical properties as indicated by their resistance to solubilization even under strongly denaturing conditions. Recent studies of Ascaris suum have demonstrated the presence of tyrosine-derived cross-links, dityrosine and isotrityrosine, that may form the linkage between subunits in assemblage of the collagenous and non-collagenous structural components of the cuticle. A peroxidase enzyme has been implicated in the synthesis of these cross-links. Recent 125I labeling studies of Haemonchus contortus have identified and characterized stage-specific proteins on the cuticular surface.