Molecular cloning and characterization of Hymenolepis diminuta α-tubulin gene

Abstract

To isolate a full-length α-tubulin cDNA from an eucestode, Hymenolepis diminuta, a lambda phage cDNA library was constructed. The α-tubulin gene was cloned, sequenced and characterized. The H. diminuta α-tubulin consisted of 450 amino acids. This protein contained putative sites for all posttranslational modifications as detyrosination/tyrosination at the carboxyl-terminal of protien, phosphorylation at residues R⁷⁹ and K³³⁶, glycylation/glutamylation at residue G⁴⁴⁵ and acetylation at residue K⁴⁰. Comparisons of H. diminuta α-tubulin with all full-length α-tubulin proteins revealed that H. diminuta α-tubulin possesses 10 distinctive residues, which are not found in any other α-tubulins. Phylogenetic analysis showed that H. diminuta α-tubulin has grouped in a separated branch adjacent eucestode and trematodes branch with 92% bootstrap value (1000 replicates). In conclusion, this is the first report of H. diminuta cDNA library construction, cloning and characterization of H. diminuta α-tubulin gene.

• Cestode
• Hymenolepis diminuta
• α-tubulin
• cDNA library
• molecular cloning

Abbreviations
Con	=	conservative substitution
Non-con	=	non-conservative substitution

Abbreviations
Con	=	conservative substitution
Non-con	=	non-conservative substitution

Notes

^*Nucleotide sequence data reported in this study are deposited in the GenBank database under accession number AF482688.

^† National organization responsible for setting and maintaining standards for the care and use of animals in research teaching and testing throughout Canada (www.ccac.ca).