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Immunoscreening of a cDNA expression library identified a 2\u00b735 kbp clone which contains a complete open reading frame encoding a protein of 653 amino acids with a predicted molecular mass of 71 kDa. Protein sequence analyses revealed 45\u201365% identity with hsp70s from a broad range of organisms, the highest homology being with the mammalian BiP (immunoglobulin heavy chain binding protein). The 69 kDa trypanosome protein shares with other BiP-related molecules two characteristics that are associated with their localization in the endoplasmic reticulum and their function as chaperonins, i.e. a hydrophobic N-terminal signal sequence and a conserved C-terminal tetrapeptide (X)DEL. Divergence between the 69 kDa antigen and other BiP-homologues occurs in the C-terminal region. This may be responsible for the high immunogenicity of the trypanosome protein. The gene for the 69 kDa antigen appears to be present as a cluster of several copies which are not organized in tandem repeats. It is expressed in all developmental stages of<jats:italic>T. congolense<\/jats:italic>, but the specific mRNA levels are higher in metacyclics than in other stages.<\/jats:p>","DOI":"10.1017\/s0031182000076277","type":"journal-article","created":{"date-parts":[[2009,6,5]],"date-time":"2009-06-05T13:55:23Z","timestamp":1244210123000},"page":"163-173","source":"Crossref","is-referenced-by-count":12,"title":["A 69 kDa immunodominant antigen of<i>Trypanosoma (Nannomonas) congolense<\/i>is homologous to immunoglobulin heavy chain binding protein 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