{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T08:06:00Z","timestamp":1790755560665,"version":"4.1.0"},"reference-count":79,"publisher":"Wiley","issue":"19","license":[{"start":{"date-parts":[[2017,9,6]],"date-time":"2017-09-06T00:00:00Z","timestamp":1504656000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100003562","name":"Ministry of Environment","doi-asserted-by":"publisher","award":["201300030002"],"award-info":[{"award-number":["201300030002"]}],"id":[{"id":"10.13039\/501100003562","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2017,10]]},"abstract":"<jats:p>Recent studies suggest that vertebrate and invertebrate defensins have evolved from two independent ancestors, and that both defensins could share origins with animal toxins. Here, we purified novel sea anemone neurotoxin (<jats:styled-content style=\"fixed-case\">BDS<\/jats:styled-content>)\u2010like antimicrobial peptides (<jats:styled-content style=\"fixed-case\">AMP<\/jats:styled-content>s)\u2014Crassicorin\u2010I and its putative homolog (Crassicorin\u2010<jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>)\u2014from the pharynx extract of an anthozoan sea anemone (<jats:italic>Urticina crassicornis<\/jats:italic>). Based on structural analyses and <jats:styled-content style=\"fixed-case\">cDNA<\/jats:styled-content> cloning, mature Crassicorin\u2010I represents a cationic <jats:styled-content style=\"fixed-case\">AMP<\/jats:styled-content> likely generated from a precursor and comprising 40 amino acid residues, including six cysteines forming three intramolecular disulfide bonds. Recombinant Crassicorin\u2010I produced in a heterologous bacterial\u2010expression system displayed antimicrobial activity against both a gram\u2010positive bacterium (<jats:italic>Bacillus subtilis<\/jats:italic>) and gram\u2010negative bacteria (<jats:italic>Escherichia coli<\/jats:italic> and <jats:italic>Salmonella enterica<\/jats:italic>). The Crassicorin\u2010I transcript was upregulated by immune challenge, suggesting its involvement in defense mechanisms against infectious pathogens in sea anemone. Sequence alignment and three\u2010dimensional molecular modeling revealed that Crassicorin\u2010I exhibits high degrees of structural similarity to sea anemone neurotoxins that share \u03b2\u2010defensin fold which is found in vertebrate defensins and invertebrate big\u2010defensins. Consistent with its structural similarity to neurotoxins, Crassicorin\u2010I exhibited paralytic activity toward a crustacean. These findings motivated our investigation and subsequent discovery of antimicrobial activity from other known sea anemone neurotoxins, such as <jats:styled-content style=\"fixed-case\">APET<\/jats:styled-content>x1 and ShK. Collectively, our work signified that Crassicorin\u2010I is the first <jats:styled-content style=\"fixed-case\">AMP<\/jats:styled-content> identified from a sea anemone and provided evidence of a functional linkage between <jats:styled-content style=\"fixed-case\">AMP<\/jats:styled-content>s and neurotoxins in a basally branching metazoan.<\/jats:p>","DOI":"10.1111\/febs.14194","type":"journal-article","created":{"date-parts":[[2017,8,10]],"date-time":"2017-08-10T11:52:43Z","timestamp":1502365963000},"page":"3320-3338","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Defensin\u2010neurotoxin dyad in a basally branching metazoan sea anemone"],"prefix":"10.1111","volume":"284","author":[{"given":"Chan\u2010Hee","family":"Kim","sequence":"first","affiliation":[{"name":"Department of Biotechnology College of Fisheries Sciences Pukyong National University Busan 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