Primary structure of a BiP homologue in Eimeria spp

• Published in: Parasitology research (1987) Vol. 82; no. 6; p. 566
• Main Authors: Dunn, P P, Bumstead, J M, Tomley, F M
• Format: Journal Article
• Language: English
• Published: Germany 1996
• Subjects: Amino Acid Sequence; Animals; Antigens, Protozoan - chemistry; Antigens, Protozoan - genetics; Antigens, Protozoan - immunology; Base Sequence; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - immunology; Chickens; DNA, Protozoan; Eimeria - genetics; Eimeria - immunology; Eimeria tenella - genetics; Eimeria tenella - immunology; Heat-Shock Proteins; Humans; Immunoglobulin Heavy Chains; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - immunology; Molecular Sequence Data; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - immunology; Sequence Homology, Amino Acid
• ISSN: 0932-0113
• DOI: 10.1007/s004360050163

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.