Worm Breeder's Gazette 9(1): 53
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
Cuticles isolated from second-stage juveniles and adult females of the plant-parasitic nematode, Meloidogyne incognita, were purified by treatment with 1% sodium dodecyl sulfate (SDS). The juvenile cuticle was composed of three zones that differed in their solubility in - mercaptoethanol (BME). Proteins in the cortical and median zones were partially soluble in BME whereas the striated basal zone was less solubilized. The BME-soluble proteins from the juvenile cuticle were separated into 12 bands by SDS-polyacrylamide gel electrophoresis and characterized as collagenous proteins based on their sensitivity to collagenase and amino acid composition (high concentrations of glycine, alanine, cysteine, and proline). The adult cuticle consisted of two zones which were solubilized extensively by BME. The basal zone which lacked the striations observed in the juvenile cuticle was completely solubilized leaving behind a network of fibers corresponding to the cortical zone. The BME-soluble proteins from the adult cuticle were separated into 9 bands electrophoretically of which one band constituted >75% (molecular weight of 76,000) of the total BME-soluble proteins. All bands were characterized as collagenous proteins. Collagenous proteins from juvenile cuticles also contained glycoproteins which were absent in the adult cuticles. Antiserum prepared against the major protein found in adult female cuticles reacted with collagenous proteins from M. incognita juveniles and Caenorhabditis