Five Different Piscidins from Nile Tilapia, Oreochromis niloticus: Analysis of Their Expressions and Biological Functions
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{"title"=>"Five Different Piscidins from Nile Tilapia, Oreochromis niloticus: Analysis of Their Expressions and Biological Functions", "type"=>"journal", "authors"=>[{"first_name"=>"Kuan Chieh", "last_name"=>"Peng", "scopus_author_id"=>"24773584200"}, {"first_name"=>"Shu Hua", "last_name"=>"Lee", "scopus_author_id"=>"57192514002"}, {"first_name"=>"Ai Ling", "last_name"=>"Hour", "scopus_author_id"=>"15839659100"}, {"first_name"=>"Chieh Yu", "last_name"=>"Pan", "scopus_author_id"=>"35488677300"}, {"first_name"=>"Lin Han", "last_name"=>"Lee", "scopus_author_id"=>"55510405600"}, {"first_name"=>"Jyh Yih", "last_name"=>"Chen", "scopus_author_id"=>"56008627700"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"23226256", "sgr"=>"84870607173", "doi"=>"10.1371/journal.pone.0050263", "scopus"=>"2-s2.0-84870607173", "pui"=>"366207246", "issn"=>"19326203"}, "id"=>"5b128379-bcc6-3cef-8ce3-f7bb6a3f9938", "abstract"=>"Piscidins are antimicrobial peptides (AMPs) that play important roles in helping fish resist pathogenic infections. Through comparisons of tilapia EST clones, the coding sequences of five piscidin-like AMPs (named TP1∼5) of Nile tilapia, Oreochromis niloticus, were determined. The complete piscidin coding sequences of TP1, -2, -3, -4, and -5 were respectively composed of 207, 234, 231, 270, and 195 bases, and each contained a translated region of 68, 77, 76, 89, and 64 amino acids. The tissue-specific, Vibrio vulnificus stimulation-specific, and Streptococcus agalactiae stimulation-specific expressions of TP2, -3, and -4 mRNA were determined by a comparative RT-PCR. Results of the tissue distribution analysis revealed high expression levels of TP2 mRNA in the skin, head kidneys, liver, and spleen. To study bacterial stimulation, S. agalactiae (SA47) was injected, and the TP4 transcript was upregulated by >13-fold (compared to the wild-type (WT) control, without injection) and was 60-fold upregulated (compared to the WT control, without injection) 24 h after the S. agalactiae (SA47) injection in the spleen and gills. Synthesized TP3 and TP4 peptides showed antimicrobial activities against several bacteria in this study, while the synthesized TP1, -2, and -5 peptides did not. The synthesized TP2, -3, and -4 peptides showed hemolytic activities and synthesized TP3 and TP4 peptides inhibited tilapia ovary cell proliferation with a dose-dependent effect. In summary, the amphiphilic α-helical cationic peptides of TP3 and TP4 may represent novel and potential antimicrobial agents for further peptide drug development.", "link"=>"http://www.mendeley.com/research/five-different-piscidins-nile-tilapia-oreochromis-niloticus-analysis-expressions-biological-function", "reader_count"=>29, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Student > Doctoral Student"=>4, "Researcher"=>2, "Student > Ph. D. Student"=>7, "Student > Postgraduate"=>2, "Student > Master"=>8, "Other"=>1, "Student > Bachelor"=>3}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Student > Doctoral Student"=>4, "Researcher"=>2, "Student > Ph. D. Student"=>7, "Student > Postgraduate"=>2, "Student > Master"=>8, "Other"=>1, "Student > Bachelor"=>3}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>22, "Medicine and Dentistry"=>1, "Veterinary Science and Veterinary Medicine"=>1, "Chemical Engineering"=>1, "Chemistry"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>22}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Chemical Engineering"=>{"Chemical Engineering"=>1}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "group_count"=>2}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/286998", "https://ndownloader.figshare.com/files/287019", "https://ndownloader.figshare.com/files/287036", "https://ndownloader.figshare.com/files/287273", "https://ndownloader.figshare.com/files/287655", "https://ndownloader.figshare.com/files/287703", "https://ndownloader.figshare.com/files/287749"], "description"=>"<div><p>Piscidins are antimicrobial peptides (AMPs) that play important roles in helping fish resist pathogenic infections. Through comparisons of tilapia EST clones, the coding sequences of five piscidin-like AMPs (named TP1∼5) of Nile tilapia, <em>Oreochromis niloticus</em>, were determined. The complete piscidin coding sequences of TP1, -2, -3, -4, and -5 were respectively composed of 207, 234, 231, 270, and 195 bases, and each contained a translated region of 68, 77, 76, 89, and 64 amino acids. The tissue-specific, <em>Vibrio vulnificus</em> stimulation-specific, and <em>Streptococcus agalactiae</em> stimulation-specific expressions of TP2, -3, and -4 mRNA were determined by a comparative RT-PCR. Results of the tissue distribution analysis revealed high expression levels of TP2 mRNA in the skin, head kidneys, liver, and spleen. To study bacterial stimulation, <em>S. agalactiae</em> (SA47) was injected, and the TP4 transcript was upregulated by >13-fold (compared to the wild-type (WT) control, without injection) and was 60-fold upregulated (compared to the WT control, without injection) 24 h after the <em>S. agalactiae</em> (SA47) injection in the spleen and gills. Synthesized TP3 and TP4 peptides showed antimicrobial activities against several bacteria in this study, while the synthesized TP1, -2, and -5 peptides did not. The synthesized TP2, -3, and -4 peptides showed hemolytic activities and synthesized TP3 and TP4 peptides inhibited tilapia ovary cell proliferation with a dose-dependent effect. In summary, the amphiphilic α-helical cationic peptides of TP3 and TP4 may represent novel and potential antimicrobial agents for further peptide drug development.</p> </div>", "links"=>[], "tags"=>["piscidins", "nile", "expressions", "functions"], "article_id"=>116556, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0050263.s001", "https://dx.doi.org/10.1371/journal.pone.0050263.s002", "https://dx.doi.org/10.1371/journal.pone.0050263.s003", "https://dx.doi.org/10.1371/journal.pone.0050263.s004", "https://dx.doi.org/10.1371/journal.pone.0050263.s005", "https://dx.doi.org/10.1371/journal.pone.0050263.s006", "https://dx.doi.org/10.1371/journal.pone.0050263.s007"], "stats"=>{"downloads"=>23, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Five_Different_Piscidins_from_Nile_Tilapia_Oreochromis_niloticus_Analysis_of_Their_Expressions_and_Biological_Functions__/116556", "title"=>"Five Different Piscidins from Nile Tilapia, <em>Oreochromis niloticus</em>: Analysis of Their Expressions and Biological Functions", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-11-30 01:49:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/532668"], "description"=>"<p>Hemolytic activities of Nile tilapia piscidin 1∼5 (TP1, -2, -3, -4, and -5) peptides against fish erythrocytes. Data (mean ± standard error) with different letters significantly differ (<i>p</i><0.05) among the experimental groups.</p>", "links"=>[], "tags"=>["immunology", "marine and aquatic sciences", "biotechnology", "pathology"], "article_id"=>203162, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.g005", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Hemolytic_activity_/203162", "title"=>"Hemolytic activity.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-30 00:52:42"}
  • {"files"=>["https://ndownloader.figshare.com/files/532333"], "description"=>"<p>A Schiffer-Edmunson plot of (a) Nile tilapia piscidin 1 (TP1), (b) -2, (c) -3, (d) -4, and (e) -5 was produced with the PEPWHEEL program. Amino acid residues are successively numbered and connect each amino acid following the sequence with lines that represent its relative position along the helix. Red indicates hydrophilic, green indicates hydrophobic, blue triangles indicate negatively charged, and blue pentagons indicate positively charged residues. Structural models of (f) TP1∼5. Pictures were generated with the Viewerlite program (Accelrys, San Diego, CA, USA).</p>", "links"=>[], "tags"=>["structures", "three-dimensional", "nile", "tilapia"], "article_id"=>202824, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.g003", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Amphipathic_945_helical_structures_and_three_dimensional_structures_of_five_different_Nile_tilapia_piscidins_/202824", "title"=>"Amphipathic α-helical structures and three-dimensional structures of five different Nile tilapia piscidins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-30 00:47:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/532162"], "description"=>"<p>Multiple sequence alignments of the Nile tilapia piscidin peptides with selected piscidin or with other members of the piscidin family. Gaps were inserted to obtain maximum homology. Sequences used for comparison with the references for GenBank accession numbers are described in Supplementary Table 3. All gene sequences of the coding region were input into the dendogram for alignment. The same amino acid is indicated by the same color, such as methionine (M) being indicated by yellow.</p>", "links"=>[], "tags"=>["alignment"], "article_id"=>202658, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.g002", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequence_alignment_between_piscidins_/202658", "title"=>"Sequence alignment between piscidins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-30 00:44:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/532733"], "description"=>"<p>Fish cells (tilapia ovary (TO2) cell line) were treated with different doses of piscidin peptides (TP1∼5) for 24 h, followed by an MTS assay. Each concentration was repeated in eight wells for three independent experiments. Piscidin treatment affected cell viability in a dose-dependent manner. There were significant differences between treatment groups for (a) TP3 (40 µg/ml) and (b) TP4 (12 µg/ml) compared to 0 µg/ml treatment. There were significant differences between treatment groups for the lower concentrations in (c) TP2 (30 µg/ml) and TP5 (10 µg/ml) compared to 0 µg/ml treatment. But survival of cells treated with 100 µg/ml of TP1, -2, and -5 were still >80%. Data are from three separate experiments. Data (mean ± SE) with different letters significantly differ (<i>p</i><0.05) among the experimental groups.</p>", "links"=>[], "tags"=>["piscidins"], "article_id"=>203229, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.g006", "stats"=>{"downloads"=>2, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effects_of_piscidins_on_cell_proliferation_/203229", "title"=>"Effects of piscidins on cell proliferation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-30 00:53:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/532519"], "description"=>"<p>(a) A qRT-PCR analysis of Nile tilapia piscidins (TP2, -3, and -4) and ubiquitin expression in various tissues (gills, liver, intestines, skin, head kidneys (abbreviated as ‘kidneys’), and spleen) of Nile tilapia. (b) qRT-PCR analysis of Nile tilapia piscidin transcripts in various tissues (gills, liver, intestines, skin, kidney, and spleen) at two time points (24 and 48 h) after an intraperitoneal injection of <i>Streptococcus agalactiae</i> (SA47) or <i>Vibrio vulnificus</i> (204). Wild-type (WT) indicates no bacteria were injected, and the fish experienced no injection. Expression data are presented as the mean (± standard error; SE) relative quantity normalized to ubiquitin. Relative quantities were calculated to the individual (WT) with the lowest normalized piscidin expression. Data (mean ± SE) with different letters significantly differ (<i>p</i><0.05) among tissues for single-gene comparisons.</p>", "links"=>[], "tags"=>["expressions", "nile", "tilapia", "piscidin", "genes", "tissues", "stimulation"], "article_id"=>203004, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.g004", "stats"=>{"downloads"=>2, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Differential_expressions_of_Nile_tilapia_piscidin_genes_in_tissues_and_after_stimulation_with_bacteria_/203004", "title"=>"Differential expressions of Nile tilapia piscidin genes in tissues and after stimulation with bacteria.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-30 00:50:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/531963"], "description"=>"<p>a. Comparison of the genomic organization of piscidin genes of Nile tilapia. The five Nile tilapia piscidin genes were located between the ninth and tenth exons of exostosin-1a-like. Both were transcribed in reverse. b. The length of the coding sequence of each exon is indicated by numbers above the boxes, and each intron is indicated by numbers above the line. Red indicates regions of translated amino acid sequences, and gray indicates the 5′ and 3′ untranslated regions (UTRs).</p>", "links"=>[], "tags"=>["nile", "tilapia", "piscidin"], "article_id"=>202454, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.g001", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Genomic_structure_and_location_of_Nile_tilapia_piscidin_genes_/202454", "title"=>"Genomic structure and location of Nile tilapia piscidin genes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-30 00:40:54"}
  • {"files"=>["https://ndownloader.figshare.com/files/532841"], "description"=>"<p>The MIC units are in µg/ml.</p>", "links"=>[], "tags"=>["nile", "tilapia", "piscidin", "peptides", "gram-positive", "-negative"], "article_id"=>203332, "categories"=>["Inorganic Chemistry", "Biotechnology", "Cell Biology", "Immunology"], "users"=>["Kuan-Chieh Peng", "Shu-Hua Lee", "Ai-Ling Hour", "Chieh-Yu Pan", "Lin-Han Lee", "Jyh-Yih Chen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050263.t001", "stats"=>{"downloads"=>2, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Activities_of_Nile_tilapia_piscidin_1_8764_5_TP1_2_3_4_and_5_peptides_against_gram_positive_and_negative_bacteria_/203332", "title"=>"Activities of Nile tilapia piscidin 1∼5 (TP1, -2, -3, -4, and -5) peptides against gram-positive and -negative bacteria.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-11-30 00:55:32"}

PMC Usage Stats | Further Information

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Relative Metric

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