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A tegument-specific venom allergen-like protein of Clonorchis sinensis.

Authors
 Hea Sun Woo  ;  Tae Yun Kim  ;  Woon-Mok Sohn  ;  Tai-Soon Yong 
Citation
 PARASITOLOGY RESEARCH, Vol.114(1) : 329-333, 2015 
Journal Title
 PARASITOLOGY RESEARCH 
ISSN
 0932-0113 
Issue Date
2015
MeSH
Allergens ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cloning, Molecular ; Clonorchis sinensis/chemistry* ; Clonorchis sinensis/genetics ; DNA, Complementary ; Female ; Helminth Proteins/analysis* ; Helminth Proteins/chemistry* ; Helminth Proteins/genetics ; Helminth Proteins/isolation & purification ; Host-Parasite Interactions ; Immunohistochemistry ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Molecular Sequence Data ; Ovum/chemistry ; Phylogeny ; Protein Structure, Tertiary ; Schistosoma mansoni/genetics ; Sequence Alignment
Keywords
Clonorchis sinensis ; SCP/TAPS ; VAL protein ; Tegument
Abstract
Venom allergen-like (VAL) proteins, members of the SCP/TAPS (sperm coating protein/Tpx-1/Ag5/PR-1/Sc7) protein superfamily, have been reported from several parasitic helminths. As little is known about their biological functions, a VAL protein of the Chinese liver fluke Clonorchis sinensis was cloned and characterized. A complementary DNA (cDNA) encoding a 25-kDa protein was identified from an EST database of C. sinensis. A BLAST search revealed that the protein shares 46% sequence identity with Schistosoma mansoni VAL 13 protein, and thus, the protein was named CsVAL13. Multiple sequence alignment indicated that the SCP/TAPS domain of CsVAL13 shares 39-46% sequence identity with VAL proteins from parasitic helminths. His and Tyr, which help to stabilize protein structure, were highly conserved across the VAL protein sequences. Phylogenetic analysis showed that the SCP/TAPS domain of the CsVAL13 sequence clusters together with other group 2 VAL protein sequences. In the homology-modeled structure of CsVAL13, an α-β-α sandwich and residues for a putative active site were highly conserved. Immune sera were obtained from BALB/c mice immunized with the recombinant CsVAL13 protein. Immunohistochemical localization using the immune sera revealed that CsVAL13 was distributed mainly in the tegument and intrauterine eggs of adult C. sinensis. These findings suggest that CsVAL13 may be involved in host-parasite interactions and immune stimulation on the surrounding host environments.
Full Text
http://link.springer.com/article/10.1007%2Fs00436-014-4212-2
DOI
10.1007/s00436-014-4212-2.
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Kim,​ Tae Yun(김태윤)
Yong, Tai Soon(용태순) ORCID logo https://orcid.org/0000-0002-3445-0769
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/139687
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