A carbohydrate epitope expressed uniquely on the cell surface of Drosophila neurons is altered in the mutant nac (neurally altered carbohydrate)

EMBO J. 1988 Nov;7(11):3471-7.

Abstract

Antibodies against horseradish peroxidase (anti-HRP) recognize neural specific cell surface antigens in Drosophila and other insects. The nature of these antigens was investigated in Drosophila and found to include a complex set of developmentally regulated proteins. Their common epitope appears to be a carbohydrate that shares features with the sugar moiety of pineapple stem bromelain, a plant glycoprotein whose carbohydrate structure has been determined. A mutation was identified that eliminates staining by the antibody in imaginal and adult neural tissue. Tissue specific glycoconjugates, although widespread in the animal kingdom, are little understood. This mutation provides a unique opportunity to address the consequences of altering a neural specific carbohydrate moiety in an otherwise intact and behaving animal. The mutation maps to 84F. A second mutation, contained on the third chromosome balancer, TM3, eliminates anti-HRP staining in embryos. These mutations appear to be separate genes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Surface / analysis*
  • Antigens, Surface / genetics
  • Bromelains / analysis
  • Carbohydrates / genetics
  • Carbohydrates / immunology*
  • Drosophila
  • Electrophoresis, Polyacrylamide Gel
  • Epitopes / analysis
  • Epitopes / genetics
  • Fluorescent Antibody Technique
  • Glycoconjugates / analysis
  • Horseradish Peroxidase / immunology
  • Mutation
  • Neurons / immunology*
  • Phenotype
  • Precipitin Tests

Substances

  • Antigens, Surface
  • Carbohydrates
  • Epitopes
  • Glycoconjugates
  • Bromelains
  • Horseradish Peroxidase