Isolation of a gene family that encodes the porin-like proteins from the human parasitic nematode Trichuris trichiura
| Autor: | D.A.P. Bundy, G.C. Barker |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Trichuris
Protein family Molecular Sequence Data Porins Protein Sorting Signals Evolution Molecular Molecular evolution Complementary DNA Gene duplication Genetics Animals Humans Amino Acid Sequence Disulfides Cloning Molecular Gene Genes Helminth Phylogeny biology Exons Helminth Proteins General Medicine biology.organism_classification Introns Porin Trichuris trichiura |
| Zdroj: | Gene. 229:131-136 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/s0378-1119(99)00039-6 |
| Popis: | The major E/S protein of Trichuris trichiura, the human whipworm, is a highly immunogenic 47-kDa protein that has a pore forming activity that is thought to be essential for the attachment of the worm to host mucosal epithelium. By gene analysis, we have demonstrated that this protein belongs to a multigene family, and we have obtained genomic and cDNA information for two of these genes. The encoded proteins are composed of tandem arrays of alternating 50- and 51-amino-acid domains within which the positioning of the cysteine residues is highly conserved. This structure resembles that of four disulphide core domain proteins, such as secretory leucocyte proteinase-1 (SLP-1), but the Trichuris protein family differs in being composed of multiple domains of this type (nine in TT50, 17 in TT95). An analysis of the relationship between the domains, and a comparison of the fine arrangement of the genes, suggests that TT95 has arisen relatively recently following duplication of the TT50 gene, which itself arose by duplication of a SLP-1-like ancestor. |
| Databáze: | OpenAIRE |
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