title: Mutations with sensory ray defect unmask cuticular glycoprotein antigens in Caenorhabditis elegans male tail.
abstract: Caenorhabditis elegans male tail has nine pairs of bilaterally symmetric ray processes extended into a cuticular fan. The formation of these structures involves both cell lineage differentiation and cellular morphogenesis. Nine mutations were examined, all of which presented an amorphous ray phenotype. Glycoconjugates carrying an N-acetylglucosamine (GlcNAc) epitope were detected at a high level in their male bursa. It was shown that these antigens are not responsible for the morphological defects. It was further demonstrated that these ram and mab gene products represent critical components for male tail cuticle organization. Mutations of them abolish the integrity of the male bursal cuticle and unmask the underlying GlcNAc epitope.
authors.affiliation: Department of Biology, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, China.
authors.forename: F C
authors.initials: FC
authors.lastname: Ko
authors.forename: K L
authors.initials: KL
authors.lastname: Chow
mesh_terms: D000818:Animals; D000947:Antigens, Helminth / Q000096:biosynthesis / Q000502:physiology; D017173:Caenorhabditis elegans / Q000196:embryology* / Q000378:metabolism; D016650:Fluorescein-5-isothiocyanate / Q000031:analogs & derivatives; D006023:Glycoproteins / Q000096:biosynthesis / Q000502:physiology*; D006031:Glycosylation; D015801:Helminth Proteins / Q000096:biosynthesis / Q000502:physiology*; D007814:Larva; D008297:Male; D018978:Molting; D009024:Morphogenesis; D016296:Mutagenesis; D010641:Phenotype; D013194:Staining and Labeling / Q000379:methods; D013623:Tail / Q000196:embryology; D014909:Wheat Germ Agglutinins
chemical_list: D000947:Antigens, Helminth; D006023:Glycoproteins; D015801:Helminth Proteins; D014909:Wheat Germ Agglutinins; C047939:fluorescein isothiocyanate-wheat germ agglutinin; D016650:Fluorescein-5-isothiocyanate