CHARACTERIZATION OF A 14 KDA OOCYST WALL PROTEIN OF EIMERIA-TENELLA AND E-ACERVULINA

We have extracted a protein of 14 kDa from purified oocyst walls of se veral Eimeria species. Polyclonal antibodies were raised in rats again st the 14 kDa proteins of E. acervulina and E. tenella. On immunoblots these antisera reacted in a highly specific manner with the homologou s 14 kDa antigens, but not with heterologous antigens. In addition, sp ecific binding of the two antisera to oocyst wall fragments of E. acer vulina and E. tenella was demonstrated by immunofluorescence. Partial amino-terminal sequences comprising 20 amino acid residues were obtain ed from the 14 kDa oocyst wall proteins of E. acervulina and E. tenell a. They are characterized by an abundance of amino acids containing hy droxyl groups in their side chains (serine, tyrosine, threonine). Bind ing of the oocyst wall protein of E. tenella by peanut agglutinin indi cates the presence of O-linked carbohydrates.