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Primary structure of a BiP homologue in Eimeria spp.

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Abstract

 cDNA clones for homologues of a molecular chaperone of the endoplasmic reticulum called the immunoglobulin heavy-chain binding protein (BiP) have been isolated from Eimeria maxima and E. tenella sporozoite cDNA libraries. The E. tenella cDNA clone is of full length and has a predicted N-terminal signal sequence of approximately 30 amino acids and a C-terminal tetrapeptide sequence (His-Asp-Glu-Leu) for retention in the lumen of the endoplasmic reticulum.

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Authors and Affiliations

  1. Institute for Animal Health, Compton, Newbury,Berkshire, RG20 0NN, UK, fax: (44-1635) 577263, e-mail: tomley@bbsrc.ac.uk, , , , , , GB

    Paul P. J. Dunn, Janene M. Bumstead & F. M. Tomley

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  1. Paul P. J. Dunn
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  2. Janene M. Bumstead
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  3. F. M. Tomley
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Received: 30 November 1995 / Accepted: 15 January 1996

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Dunn, P., Bumstead, J. & Tomley, F. Primary structure of a BiP homologue in Eimeria spp.. Parasitol Res 82, 566–568 (1996). https://doi.org/10.1007/s004360050163

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  • DOI: https://doi.org/10.1007/s004360050163

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