JBC, Vol. 251, Issue 2, 302-307, Jan, 1976
Studies of a glycoprotein in the oocysts of Eimeria tenella
R. L. Stotish, C. C. Wang, M. Hichens, W. J. VandenHeuvel and P. Gale
A glycoprotein unique to the cytoplasm of the unsporulated oocyst of
Eimeria tenella has been purified and partially characterized. The protein
has a molecular weight of 30,000, of which approximately 40% is
carbohydrate. The carbohydrate portion of the molecule consists of glucose,
galactose, mannose, xylose, glucosamine, and galactosamine, with no
detectable sialic acid. The protein portion contains approximately 141
residues, being rich in hydrophilic amino acids with very few aromatic
amino acids and no cystine. The protein comprises 14% of the total soluble
protein of the unsporulated oocyst but has not been identified in the
cytoplasm of any other developmental stage of the organism. Using
polyacrylamide gel electrophoresis and a radioimmunoassay specific for the
protein, it has been shown to disappear from the cytoplasm between the 15th
and 20th hour of the 20-hour sporulation process. Subsequent
immunofluorescence experiments have shown a reactive material as a
component of the sporozoite membrane. These results indicate that the
glycoprotein is a structural protein of the sporozoite membrane, apparently
synthesized by the unsporulated oocyst and incorporated into the sporozoite
membrane as one of the last steps involved in the sporulation process.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
