Characterization of a 14 kDa oocyst wall protein ofEimeria tenellaandE. acervulina

Abstract

SummaryWe have extracted a protein of 14 kDa from purified oocyst walls of severalEimeriaspecies. Polyclonal antibodies were raised in rats against the 14 kDa proteins ofE. acervulinaandE. tenella. On immunoblots these antisera reacted in a highly specific manner with the homologous 14 kDa antigens, but not with heterologous antigens. In addition, specific binding of the two antisera to oocyst wall fragments ofE. acervulinaandE. tenellawas demonstrated by immunofluorescence. Partial amino-terminal sequences comprising 20 amino acid residues were obtained from the 14 kDa oocyst wall proteins ofE. acervulinaandE. tenella. They are characterized by an abundance of amino acids containing hydroxyl groups in their side chains (serine, tyrosine, threonine). Binding of the oocyst wall protein ofE. tenellaby peanut agglutinin indicates the presence of O-linked carbohydrates.