Mass spectrometric analysis of particular proteins of thai paragonimus heterotremus worms

Abstract

Paragonimus heterotremus is the causative agent of human paragonimiasis in Thailand. The protein molecular weights (MW) of 32.5, 33 and 35 kDa were used as diagnosis bands, and were reacted with human paragonimiasis sera confirmed by the presence of eggs and parasites, for immunoblotting. To study biological systems of the immunodominant worm antigen, protein MWs at 25-50 kDa were analyzed by Mass Spectrometry, Scaffold Version 4 and Blast2go against NCBI. The Top-Hit species were Clonorchissinensis, Schistosoma japonicum, Schistosoma mansoni, Paragonimus westermani, Fasciola hepatica and other parasites. The sequence distribution of molecular function indicated that most functions were binding, catalytic activity or ion binding. Mass Spectrometry data showed that proteins at 32.5, 33 and 35 kDa were succinate dehydrogenase complex, subunit B, iron sulfur [Schistosoma japonicum], actin beta/gamma 1 [Clonorchis sinensis] and tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein [Clonorchis sinensis]. This study aimed to understand more about the antigenic proteins of P. heterotremus in terms of protein identification, functions and their components. This data will also be used to develop and produce new types of antigen for immunodiagnostic applications.