Abstract:
:Infectivity of the multicellular pathogen Schistosoma mansoni for the human host is dependent upon the ability of free-living cercariae to transform rapidly into parasitic schistosomula. The biochemical pathways that regulate this transitional period are unknown. The role of protein phosphorylation was investigated by examining the incorporation of [32Pi]phosphate into proteins of S. mansoni. A sevenfold increase in total phosphorylation was found in 3-hr-old schistosomula as compared to cercariae. Analysis of radiolabeled proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography demonstrated that a 14-kDa protein served as a marker for transformation, being phosphorylated in schistosomula but not cercariae. The protein was phosphorylated on a serine residue. Phosphorylation was stimulated by a shift of parasites from water to salt-containing medium at 23 degrees C. Incubation of organisms in water at 37 degrees C did not initiate phosphorylation of this protein. The 14-kDa phosphoprotein was extracted from parasite homogenates with 1 M NaCl but was insoluble in 1% Triton X-100. Protein phosphorylation during the cercarial-schistosomula transformation may represent an important biochemical event that regulates infectivity of the parasite for the human host.
journal_name
Exp Parasitoljournal_title
Experimental parasitologyauthors
Wiest PM,Olds GR,Bowen WDdoi
10.1016/0014-4894(91)90024-qkeywords:
subject
Has Abstractpub_date
1991-08-01 00:00:00pages
214-22issue
2eissn
0014-4894issn
1090-2449pii
0014-4894(91)90024-Qjournal_volume
73pub_type
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