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dc.contributor.authorKanokkarn Pothongen_US
dc.contributor.authorกนกกาญจน์ โพธิ์ทองen_US
dc.contributor.authorParon Dekumyoyen_US
dc.contributor.authorพารณ ดีคำย้อยen_US
dc.contributor.authorThareerat Kalambahetien_US
dc.contributor.authorธารีรัตน์ กะลัมพะเหติen_US
dc.contributor.authorDorn Watthanakulpanichen_US
dc.contributor.authorดร วัฒนกุลพานิชย์en_US
dc.contributor.authorChalit Komalmisraen_US
dc.contributor.authorชลิต โกมลมิศร์en_US
dc.contributor.authorTimothy P Yoshinoen_US
dc.contributor.otherMahidol University. Faculty of Tropical Medicine. Department of Helminthologyen_US
dc.contributor.otherMahidol University. Faculty of Tropical Medicine. Department of Microbiology and Immunologyen_US
dc.descriptionJoint International Tropical Medicine Meeting 2014: 3D perspectives on tropical medicine: drivers, diversity and determination the 8th seminar on food-and water-borne parasitic zoonoses: 2-4 December 2014: Centara Grand Bangkok Convention Center at Central World, Bangkok, Thailand. Bangkok: Faculty of Tropical Medicine, Mahidol University; 2014. p. 277.en
dc.description.abstractParagonimus 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.en_US
dc.rightsMahidol Universityen_US
dc.subjectParagonimus heterotremusen_US
dc.subjectMass spectrometryen_US
dc.titleMass spectrometric analysis of particular proteins of thai paragonimus heterotremus wormsen_US
dc.typeProceeding Posteren_US
Appears in Collections:TM-Proceeding Document

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