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Characterization of a 14 kDa oocyst wall protein of Eimeria tenella and E. acervulina

Published online by Cambridge University Press:  26 March 2010

K.-H. Eschenbacher ,
P. Eggli ,
M. Wallach  and
R. Braun
K.-H. Eschenbacher
Affiliation:
Institut für Allgemeine Mikrobiologie, Universität Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
P. Eggli
Affiliation:
Anatomisches Institut, Medizinische Fakultät, Universität Bern, Bühlstrasse 26, CH-3012 Bern, Switzerland
M. Wallach
Affiliation:
ABIC Ltd Pharmaceutical and Chemical Industries, Industrial Zone, Kiryat Nordau, Natanya, P. O. B. 8077, Israel
R. Braun
Affiliation:
Institut für Allgemeine Mikrobiologie, Universität Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
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Summary

We have extracted a protein of 14 kDa from purified oocyst walls of several Eimeria species. Polyclonal antibodies were raised in rats against the 14 kDa proteins of E. acervulina and E. 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 of E. acervulina and E. tenella was demonstrated by immunofluorescence. Partial amino-terminal sequences comprising 20 amino acid residues were obtained from the 14 kDa oocyst wall proteins of E. acervulina and E. 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 of E. tenella by peanut agglutinin indicates the presence of O-linked carbohydrates.

Keywords

ApicomplexaEimeriaoocyst wall proteinpolyclonal antibodiesN-terminal sequencepeanut agglutinin
Type
Research Article
Information
Parasitology , Volume 112 , Issue 2 , February 1996 , pp. 169 - 176
Copyright
Copyright © Cambridge University Press 1996

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