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Ferredoxin: A novel antimicrobial peptide derived from the black scraper (Thamnaconus modestus).
Choi, Kwang-Min; Kim, Kyung-Ho; Kang, Gyoungsik; Woo, Won-Sik; Sohn, Min-Young; Son, Ha-Jeong; Park, Chan-Il.
Afiliación
  • Choi KM; Ecological Risk Research Department, Korea Institute of Ocean Science and Technology (KIOST), Geoje, 53201, Republic of Korea; Department of Marine Biology & Aquaculture, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea.
  • Kim KH; Department of Marine Biology & Aquaculture, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea.
  • Kang G; Department of Aquatic Life Medicine, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea.
  • Woo WS; Department of Marine Biology & Aquaculture, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea.
  • Sohn MY; Department of Marine Biology & Aquaculture, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea.
  • Son HJ; Department of Marine Biology & Aquaculture, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea.
  • Park CI; Department of Marine Biology & Aquaculture, College of Marine Science, Gyeongsang National University, 455, Tongyeong, 650-160, Republic of Korea. Electronic address: pakrci@gnu.ac.kr.
Fish Shellfish Immunol ; 152: 109796, 2024 Sep.
Article en En | MEDLINE | ID: mdl-39074519
ABSTRACT
Ferredoxin (FDX) is a highly conserved iron-sulfur protein that participates in redox reactions and plays an important role as an electron transport protein in biological processes. However, its function in marine fish remains unclear. We identified two ferrodoxin proteins, FDX1 and FDX2, from black scraper (Thamnaconus modestus) to confirm their genetic structures and expression profiles and to investigate their antimicrobial activity properties by fabricating them with antimicrobial peptides based on sequences. The two TmFDXs mRNAs were most abundant in peripheral blood leukocytes of healthy T. modestus. After artificial infection with Vibrio anguillarum, a major pathogen of T. modestus, TmFDX1 mRNA was significantly upregulated in the gills, heart, intestines, kidneys, liver, and spleen, but was consistently downregulated in the brain. The expression levels of TmFDX2 mRNA were significantly upregulated in the heart, intestines, kidneys, liver, and spleen; however, no significant changes in expression were observed in the brain or gills. Based on the 2Fe-2S ferredoxin-type iron-sulfur-binding domain sequence, two peptides (pFDX1 and pFDX2) were synthesized. The bactericidal effect, biofilm formation inhibition, and gDNA-binding activity of these peptides were investigated. These findings highlight the potential as a natural peptide candidate for TmFDXs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vibrio / Vibriosis / Secuencia de Aminoácidos / Proteínas de Peces / Ferredoxinas / Enfermedades de los Peces / Péptidos Antimicrobianos Límite: Animals Idioma: En Revista: Fish Shellfish Immunol Asunto de la revista: BIOLOGIA / MEDICINA VETERINARIA Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vibrio / Vibriosis / Secuencia de Aminoácidos / Proteínas de Peces / Ferredoxinas / Enfermedades de los Peces / Péptidos Antimicrobianos Límite: Animals Idioma: En Revista: Fish Shellfish Immunol Asunto de la revista: BIOLOGIA / MEDICINA VETERINARIA Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido