Identification and characterization of pufflectin from the grass pufferfish Takifugu niphobles and comparison of its expression with that of Takifugu rubripes |
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| Affiliation: | 1. Nano-Information Technology Academy (NITA), Dongguk University, Seoul, Republic of Korea;2. Department of Physics and Nanotechnology, SRM Institute of Science and Technology, Kattankulathur, India;3. Center of Research Excellence in Corrosion, King Fahd University of Petroleum & Minerals, Saudi Arabia;4. Department of Semiconductor Science, Dongguk University-Seoul, Seoul 04620, Republic of Korea;1. Key Laboratory of Healthy Mariculture for the East China Sea, Ministry of Agriculture and Rural Affairs, Fisheries College, Jimei University, Xiamen 361021, China;2. College of Marine Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China;3. Key Laboratory of Marine Biotechnology of Fujian Province, Institute of Oceanology, Fujian Agriculture and Forestry University, Fuzhou 350002, China;4. College of Ocean and Earth Sciences, Xiamen University, Xiamen, 361005, China |
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| Abstract: | Pufflectin found in Takifugu rubripes (Tr pufflectin) is the first animal lectin reported to show sequence similarity to monocotyledonous plant lectins. In the present study, we identified and characterized an orthologous lectin from Takifugu niphobles (Tn pufflectin), a species closely related to T. rubripes. Tn pufflectin exhibits 86% identity to Tr pufflectin with two conserved mannose-binding domains. Tn pufflectin was mainly expressed in the skin, gills, brain, and muscles; however, it was expressed at a lower level in the other examined tissues. Recombinant Tn pufflectin, expressed by Escherichia coli, exhibited binding activity specific for d-mannose. The expression of pufflectin in the gills was much lower in T. niphobles than in T. rubripes; notably, the former and latter are resistant and susceptible, respectively, to the monogenean parasite Heterobothrium okamotoi, which parasitizes gills. This suggests that pufflectin might be utilized by the parasite for host recognition. |
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