Molecular characterisation and biological activity of an antiparasitic peptide from Sciaenops ocellatus and its immune response to Cryptocaryon irritans

•We identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus. So-pis is abound in glycine residues (22.7 %) and has a neutral isoelectric point.•The synthetic peptide So-pis displayed weak haemolytic activity, limited or no activity against bacteria and fung...

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Veröffentlicht in:Molecular immunology 2022-01, Vol.141, p.1-12
Hauptverfasser: Jin, Yuan, Mao, Yong, Niu, Su-Fang, Pan, Ying, Zheng, Wei-Hao, Wang, Jun
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creator Jin, Yuan
Mao, Yong
Niu, Su-Fang
Pan, Ying
Zheng, Wei-Hao
Wang, Jun
description •We identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus. So-pis is abound in glycine residues (22.7 %) and has a neutral isoelectric point.•The synthetic peptide So-pis displayed weak haemolytic activity, limited or no activity against bacteria and fungi, but potent antiparasitic activity against C. irritans.•So-pis might be involved in host defence against C. irritans infection.•So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease. Cryptocaryon irritans, a holotrichous ciliate parasitic protozoan, can trigger marine white spot disease and cause substantial economic losses in mariculture. However, methods of preventing and curing the disease have negatively affect fish, human, other organisms, and the natural environment. The antiparasitic activity of some antimicrobial peptides (AMPs) has garnered extensive attention of scholars. In this study, we identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus. The sequence analysis, structural features, and tissue distribution suggested that So-pis is genetically related to the piscidins family. However, So-pis showed a relatively low overall conservation compared with other known piscidins. So-pis is abound in glycine residues (22.7 %) and it has a neutral isoelectric point, weak amphipathicity, relatively long α-helix, and high hydrophobicity. These key elements are responsible for its biological activity. Quantitative real-time polymerase chain reaction (qRT-PCR) data indicated that So-pis is a typically gill-expressed peptide. The expression of So-pis in the gill, skin, spleen, and head kidney could be regulated during C. irritans infection, thereby implicating a role of So-pis in immune defence against C. irritans. The synthetic So-pis had limited or no antimicrobial activity against bacterial and yeasts but exhibited potent antiparasitic activity against C. irritans in vitro. The activity of synthetic So-pis against erythrocytes was less potent than its antiparasitic activity against C. irritans. These results indicated that So-pis might be one of the crucial defence cytokines against C. irritans in the red drum. Cumulatively, our data suggested that So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease.
doi_str_mv 10.1016/j.molimm.2021.08.010
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So-pis is abound in glycine residues (22.7 %) and has a neutral isoelectric point.•The synthetic peptide So-pis displayed weak haemolytic activity, limited or no activity against bacteria and fungi, but potent antiparasitic activity against C. irritans.•So-pis might be involved in host defence against C. irritans infection.•So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease. Cryptocaryon irritans, a holotrichous ciliate parasitic protozoan, can trigger marine white spot disease and cause substantial economic losses in mariculture. However, methods of preventing and curing the disease have negatively affect fish, human, other organisms, and the natural environment. The antiparasitic activity of some antimicrobial peptides (AMPs) has garnered extensive attention of scholars. In this study, we identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus. The sequence analysis, structural features, and tissue distribution suggested that So-pis is genetically related to the piscidins family. However, So-pis showed a relatively low overall conservation compared with other known piscidins. So-pis is abound in glycine residues (22.7 %) and it has a neutral isoelectric point, weak amphipathicity, relatively long α-helix, and high hydrophobicity. These key elements are responsible for its biological activity. Quantitative real-time polymerase chain reaction (qRT-PCR) data indicated that So-pis is a typically gill-expressed peptide. The expression of So-pis in the gill, skin, spleen, and head kidney could be regulated during C. irritans infection, thereby implicating a role of So-pis in immune defence against C. irritans. The synthetic So-pis had limited or no antimicrobial activity against bacterial and yeasts but exhibited potent antiparasitic activity against C. irritans in vitro. The activity of synthetic So-pis against erythrocytes was less potent than its antiparasitic activity against C. irritans. These results indicated that So-pis might be one of the crucial defence cytokines against C. irritans in the red drum. Cumulatively, our data suggested that So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease.</description><identifier>ISSN: 0161-5890</identifier><identifier>EISSN: 1872-9142</identifier><identifier>DOI: 10.1016/j.molimm.2021.08.010</identifier><identifier>PMID: 34781186</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Anti-Infective Agents - pharmacology ; Antimicrobial Cationic Peptides - pharmacology ; Antiparasitic activity ; Antiparasitic Agents - pharmacology ; Base Sequence ; Ciliophora Infections - drug therapy ; Ciliophora Infections - immunology ; Ciliophora Infections - parasitology ; Cryptocaryon irritans ; Fish Diseases - immunology ; Gills - immunology ; Gills - metabolism ; Gills - parasitology ; Hymenostomatida - drug effects ; Immune response ; Immunity - drug effects ; Novel piscidin-like ; Perciformes - immunology ; Perciformes - metabolism ; Sciaenops ocellatus</subject><ispartof>Molecular immunology, 2022-01, Vol.141, p.1-12</ispartof><rights>2021</rights><rights>Copyright © 2021. 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So-pis is abound in glycine residues (22.7 %) and has a neutral isoelectric point.•The synthetic peptide So-pis displayed weak haemolytic activity, limited or no activity against bacteria and fungi, but potent antiparasitic activity against C. irritans.•So-pis might be involved in host defence against C. irritans infection.•So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease. Cryptocaryon irritans, a holotrichous ciliate parasitic protozoan, can trigger marine white spot disease and cause substantial economic losses in mariculture. However, methods of preventing and curing the disease have negatively affect fish, human, other organisms, and the natural environment. The antiparasitic activity of some antimicrobial peptides (AMPs) has garnered extensive attention of scholars. In this study, we identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus. The sequence analysis, structural features, and tissue distribution suggested that So-pis is genetically related to the piscidins family. However, So-pis showed a relatively low overall conservation compared with other known piscidins. So-pis is abound in glycine residues (22.7 %) and it has a neutral isoelectric point, weak amphipathicity, relatively long α-helix, and high hydrophobicity. These key elements are responsible for its biological activity. Quantitative real-time polymerase chain reaction (qRT-PCR) data indicated that So-pis is a typically gill-expressed peptide. The expression of So-pis in the gill, skin, spleen, and head kidney could be regulated during C. irritans infection, thereby implicating a role of So-pis in immune defence against C. irritans. The synthetic So-pis had limited or no antimicrobial activity against bacterial and yeasts but exhibited potent antiparasitic activity against C. irritans in vitro. The activity of synthetic So-pis against erythrocytes was less potent than its antiparasitic activity against C. irritans. These results indicated that So-pis might be one of the crucial defence cytokines against C. irritans in the red drum. Cumulatively, our data suggested that So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Antiparasitic activity</subject><subject>Antiparasitic Agents - pharmacology</subject><subject>Base Sequence</subject><subject>Ciliophora Infections - drug therapy</subject><subject>Ciliophora Infections - immunology</subject><subject>Ciliophora Infections - parasitology</subject><subject>Cryptocaryon irritans</subject><subject>Fish Diseases - immunology</subject><subject>Gills - immunology</subject><subject>Gills - metabolism</subject><subject>Gills - parasitology</subject><subject>Hymenostomatida - drug effects</subject><subject>Immune response</subject><subject>Immunity - drug effects</subject><subject>Novel piscidin-like</subject><subject>Perciformes - immunology</subject><subject>Perciformes - metabolism</subject><subject>Sciaenops ocellatus</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUFv1DAQhS0Earel_wAhH7kkjJ3ETi5IaFWgUqsegLPlOBOYVRIH26m0_4Sfi9stHJEs-TDvzXujj7E3AkoBQr0_lLOfaJ5LCVKU0JYg4AXbiVbLohO1fMl2WSaKpu3gnF3EeAAABao5Y-dVrVshWrVjv-_8hG6bbODupw3WJQwUbSK_cLsMvCc_-R_k7MTzjB4oHbkf8yi_RGt2RErk-IprogH5GPzMvzqyuPg1cu9wmmza4tMySpHnxtuCPGBc_RKRJ8_34bgm72w45lAKgZJd4mv2arRTxKvn_5J9_3T9bf-luL3_fLP_eFu4SslUDIMbtYMKtK5g7GrtegtN7Wple4B-VNIB9hWoUfXYWjlaGHTX6E5aAaCr6pK9O-1dg_-1YUxmpvjUekG_RSObrgWtahBZWp-kLvgYA45mDTTn2kaAeWRiDubExDwyMdCazCTb3j4nbP2Mwz_TXwhZ8OEkwHznA2Ew0REuDgcK6JIZPP0_4Q8BM6Pi</recordid><startdate>202201</startdate><enddate>202201</enddate><creator>Jin, Yuan</creator><creator>Mao, Yong</creator><creator>Niu, Su-Fang</creator><creator>Pan, Ying</creator><creator>Zheng, Wei-Hao</creator><creator>Wang, Jun</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>202201</creationdate><title>Molecular characterisation and biological activity of an antiparasitic peptide from Sciaenops ocellatus and its immune response to Cryptocaryon irritans</title><author>Jin, Yuan ; 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So-pis is abound in glycine residues (22.7 %) and has a neutral isoelectric point.•The synthetic peptide So-pis displayed weak haemolytic activity, limited or no activity against bacteria and fungi, but potent antiparasitic activity against C. irritans.•So-pis might be involved in host defence against C. irritans infection.•So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease. Cryptocaryon irritans, a holotrichous ciliate parasitic protozoan, can trigger marine white spot disease and cause substantial economic losses in mariculture. However, methods of preventing and curing the disease have negatively affect fish, human, other organisms, and the natural environment. The antiparasitic activity of some antimicrobial peptides (AMPs) has garnered extensive attention of scholars. In this study, we identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus. The sequence analysis, structural features, and tissue distribution suggested that So-pis is genetically related to the piscidins family. However, So-pis showed a relatively low overall conservation compared with other known piscidins. So-pis is abound in glycine residues (22.7 %) and it has a neutral isoelectric point, weak amphipathicity, relatively long α-helix, and high hydrophobicity. These key elements are responsible for its biological activity. Quantitative real-time polymerase chain reaction (qRT-PCR) data indicated that So-pis is a typically gill-expressed peptide. The expression of So-pis in the gill, skin, spleen, and head kidney could be regulated during C. irritans infection, thereby implicating a role of So-pis in immune defence against C. irritans. The synthetic So-pis had limited or no antimicrobial activity against bacterial and yeasts but exhibited potent antiparasitic activity against C. irritans in vitro. The activity of synthetic So-pis against erythrocytes was less potent than its antiparasitic activity against C. irritans. These results indicated that So-pis might be one of the crucial defence cytokines against C. irritans in the red drum. Cumulatively, our data suggested that So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>34781186</pmid><doi>10.1016/j.molimm.2021.08.010</doi><tpages>12</tpages></addata></record>
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subjects Amino Acid Sequence
Animals
Anti-Infective Agents - pharmacology
Antimicrobial Cationic Peptides - pharmacology
Antiparasitic activity
Antiparasitic Agents - pharmacology
Base Sequence
Ciliophora Infections - drug therapy
Ciliophora Infections - immunology
Ciliophora Infections - parasitology
Cryptocaryon irritans
Fish Diseases - immunology
Gills - immunology
Gills - metabolism
Gills - parasitology
Hymenostomatida - drug effects
Immune response
Immunity - drug effects
Novel piscidin-like
Perciformes - immunology
Perciformes - metabolism
Sciaenops ocellatus
title Molecular characterisation and biological activity of an antiparasitic peptide from Sciaenops ocellatus and its immune response to Cryptocaryon irritans
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