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Tytuł:
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Molecular characterization of 60S ribosomal protein L12 of E. tenella.
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Autorzy:
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Liang S; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China; College of Life Sciences, Shanghai Normal University, Shanghai, 200234, China.
Zhu S; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Zhao Q; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Yu Y; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China; College of Life Sciences, Shanghai Normal University, Shanghai, 200234, China.
Dong H; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Wang Q; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Wang H; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Yu S; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Huang B; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China.
Han H; Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Key Laboratory of Animal Parasitology of Ministry of Agriculture, Minhang, Shanghai, 200241, PR China. Electronic address: .
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Źródło:
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Experimental parasitology [Exp Parasitol] 2020 Oct; Vol. 217, pp. 107963. Date of Electronic Publication: 2020 Aug 09.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Publication: Orlando, FL : Academic Press
Original Publication: New York.
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MeSH Terms:
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Eimeria tenella/*genetics
Ribosomal Proteins/*genetics
Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Western ; Cecum/parasitology ; Cell Line ; Chick Embryo ; Chickens ; Computational Biology ; DNA, Complementary/genetics ; DNA, Complementary/metabolism ; Eimeria tenella/chemistry ; Electrophoresis, Polyacrylamide Gel ; Feces/parasitology ; Fibroblasts ; Fluorescent Antibody Technique, Indirect ; Protein Biosynthesis ; Rabbits ; Real-Time Polymerase Chain Reaction ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Ribosomal Proteins/chemistry ; Specific Pathogen-Free Organisms ; Transcription, Genetic
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Contributed Indexing:
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Keywords: 60S ribosomal protein; Avian coccidiosis; Eimeria tenella
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Substance Nomenclature:
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0 (DNA, Complementary)
0 (Recombinant Proteins)
0 (Ribosomal Proteins)
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Entry Date(s):
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Date Created: 20200812 Date Completed: 20201013 Latest Revision: 20201013
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Update Code:
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20240105
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DOI:
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10.1016/j.exppara.2020.107963
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PMID:
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32781092
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This study analyzed the large-subunit (60S) ribosomal protein L12 of Eimeria tenella (Et60s-RPL12). A full-length cDNA was cloned, and the recombinant protein was expressed in E. coli BL21 and inoculated in rabbits to produce the polyclonal antibody. Quantitative real-time polymerase chain reaction and western blotting were used to analyze the transcription levels of Et60s-RPL12 and translation levels in different developmental stages of E. tenella. The results showed that the mRNA transcription level of Et60s-RPL12 was highest in second-generation merozoites, whereas the translation level was highest in unsporulated oocysts. Indirect immunofluorescence showed that Et60s-RPL12 was localized to the anterior region and surface of sporozoites, except for the two refractile bodies. As the invasion of DF-1 cells progressed, fluorescence intensity was increased, and Et60s-RPL12 was localized to the parasitophorous vacuole membrane (PVM). The secretion assay results using staurosporine indicated that this protein was secreted, but not from micronemes. The role of Et60s-RPL12 in invasion was evaluated in vitro. The results of the invasion assay showed that polyclonal antibody inhibited host cell invasion by the parasite, which reached about 12%. However, the rate of invasion was not correlated with the concentration of IgG.
(Copyright © 2020 Elsevier Inc. All rights reserved.)
