Location: Animal Parasitic Diseases
Title: TsDAF-21/Hsp90 is expressed in all examined stages of Trichinella spiralis Authors
Submitted to: Veterinary Parasitology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: October 10, 2012
Publication Date: May 20, 2013
Citation: Yang, Y., Qina, W., Zarlenga, D.S., Cao, L., Tian, G. 2013. TsDAF-21/Hsp90 is expressed in all examined stages of Trichinella spiralis. Veterinary Parasitology. 194(2-4):171-174. Interpretive Summary: Trichinella is an important and global zoonotic parasite. Organisms belonging to this genus infect a wide variety of animals most importantly, humans. Heat shock proteins (Hsp) function as molecular chaperones, are involved in many cellular processes and play key roles in the ability of an organism to respond to external stress. Hsp have been found in nematodes but little has been done to characterize Hsp in Trichinella, in particular Hsp90. To this end, preliminary work involved cloning and sequencing the Hsp90 gene, and expressing the protein such that antibodies could be generated. Results using these reagents demonstrated that both the Hsp90 gene and the protein are constitutively expressed in all life cycle stages of Trichinella and in both male and female adult worms suggesting the protein is readily available for assisting the parasite in responding to changes in its external environment. Such a gene and gene product can be instrumental to researchers in developing a target within the parasite to attenuate the growth and development of the organism and reduce transmission among food animals.
Technical Abstract: Trichinella is an important parasitic nematode of animals worldwide. Heat shock proteins are ubiquitous in nature and allow organisms to quickly respond to environmental stress. A portion of the Tsdaf-21 gene, a Caenorhabditis elegans daf-21 homologue encoding heat-shock protein 90 (Hsp90) was cloned from Trichinella spiralis. The partial nucleotide sequence resided near the 5’-end of the gene and encoded a polypeptide of 254 amino acid residues harboring a HATPase-c superfamily domain and Hsp90 protein domain. Phylogenetic analysis revealed that Tsdaf-21 is highly conserved and formed a monophyletic clade with other nematodes. The partial Tsdaf-21 transcript was subcloned and expressed for antibody production. Results using PCR primers specific for the Tsdaf-21 transcript, and mouse polyclonal antisera specific for the recombinant protein showed that both the RNA transcript and the corresponding protein were ubiquitously and consistently expressed in newborn larvae, muscle larvae and both male and female adult worms in the absence of any external stress or stimulation.