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ISSN : 1225-3480

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29권 2호

Manila clam, Ruditapes philippinarum Cathepsin D: Molecular analysis and immune response against brown ring disease causing Vibrio tapetis challenge

Manila clam, Ruditapes philippinarum Cathepsin D: Molecular analysis and immune response against brown ring disease causing Vibrio tapetis challenge

Menike, Udeni (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungnam National University)
Ariyasiri, Krishan (Department of Biology, Chungnam National University)
Choi, Jin-Young (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungnam National University)
Lee, Youngdeuk (Korea Institute of Ocean Science Technology)
Wickramaarachchi, W.D.N. (Department of Marine Life Sciences, Jeju National University)
Premachandra, H.K.A. (Department of Marine Life Sciences, Jeju National University)
Lee, Jehee (Department of Marine Life Sciences, Jeju National University)
De Zoysa, Mahanama (College of Veterinary Medicine and Research Institute of Veterinary Medicine, Chungnam National University)
한국패류학회지 / The Korean Journal of Malacology, (P)1225-3480;
2013, v.29 no.2, pp.155-161
https://doi.org/10.9710/kjm.2013.29.2.155
Menike, Udeni, Ariyasiri, Krishan, Choi, Jin-Young, Lee, Youngdeuk, Wickramaarachchi, W.D.N., Premachandra, H.K.A., Lee, Jehee, & De Zoysa, Mahanama. (2013). Manila clam, Ruditapes philippinarum Cathepsin D: Molecular analysis and immune response against brown ring disease causing Vibrio tapetis challenge. , 29(2), 155-161, https://doi.org/10.9710/kjm.2013.29.2.155

Abstract

Cathepsins are lysosomal/cysteine proteases belong to papain family (C1 family) that is involved in intracellular protein degradation, antigen processing, hormone maturation, and immune responses. In this study, member of cathepsin family was identified from Manila clam (Mc-Cathepsin D) and investigated the immune response against brown ring disease (BRD) causing Vibrio tapetis challenge. The identified Mc-Cathepsin D gene encodes characteristic features typical for the cathepsin family including eukaryotic and viral aspartyl protease signature domain and two highly conserved active sites ($^{84}VVFDTGSSNLWV^{95}$ and $^{270}IADTGTSLLAG^{281}$). Moreover, MC-Cathepsin D shows higher identity values (-50-70%) and conserved amino acids with known cathepsin D members. Transcriptional results (by quantitative real-time RT-PCR) showed that Mc-Cathepsin D was expressed at higher levels in gills and hemocytes than mantle, adductor muscle, foot, and siphon. After the V. tapetis challenge under laboratory conditions, Mc-Cathepsin D mRNA was up-regulated in gills and hemocytes. Present study indicates that Mc-Cathepsin D is constitutively expressed in different tissues and potentially inducible when infecting BRD by V. tapetis. It is further suggesting that Mc-Cathepsin D may be involved in multiple role including immune response reactions against BRD.

keywords
Brown ring disease, Manila clam (Ruditapes philipphinarum), Cathepsin D, V. tapetis

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