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.

Cuticular Collagenous Proteins of Second-Stage Juveniles and Adult Females of Meloidogyne incognita

S.R. Reddigari, P.L. Jansma, P. Devidas, and R.S. Hussey

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