Protein and antigen phosphorylation in the tegument of Schistosoma mansoni.
Incubation of male and female Schistosoma mansoni for 3-6 h in media containing [32P]phosphate indicated that a large number of proteins extending across a wide molecular weight range were phosphorylated. The nature of the phosphorylated proteins was investigated by using three methods for removal of tegumental membranes. A 94 kDa polypeptide in the tegument became rapidly phosphorylated in vivo and it was also phosphorylated by incubation of isolated tegumental membranes in [32P]ATP in the presence of a protein kinase. After incubation of parasites in vivo for longer periods, other phosphorylated polypeptides of 62, 60, 57, 32 and 28 kDa were also identified. The major phosphorylated polypeptide immunoprecipitated from schistosomes by antisera raised in mice to irradiated cercariae was 62 kDa; others, of 48, 43 and 32 kDa, were also identified, using antisera raised in mice chronically infected with cercariae. The results suggest that mechanisms for receptor-mediated transmembrane signalling occur in the tegument of schistosomes.
National Institute for Medical Research, Mill Hill, London, U.K.
E
E
Kalopothakis
F
F
Rumjanek
W H
WH
Evans
D000818:Animals; D000947:Antigens, Helminth / Q000032:analysis / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007118:Immunoassay; D008297:Male; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism*; D010750:Phosphoproteins / Q000032:analysis / Q000378:metabolism*; D010766:Phosphorylation; D012550:Schistosoma mansoni / Q000032:analysis / Q000276:immunology / Q000378:metabolism*
D000947:Antigens, Helminth; D008565:Membrane Proteins; D010750:Phosphoproteins