Myticusin-beta, antimicrobial peptide from the marine bivalve, Mytilus coruscus
We isolated and purified an antimicrobial peptide (AMP) from the mantle of the hard-shelled mussel, Mytilus coruscus. The peptide was purified through C18 reversed-phase high-performance liquid chromatography, and displayed antibacterial activity. Total molecular mass of 11,182 Da was determined usi...
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| Published in | Fish & shellfish immunology Vol. 99; pp. 342 - 352 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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England
Elsevier Ltd
01.04.2020
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| Abstract | We isolated and purified an antimicrobial peptide (AMP) from the mantle of the hard-shelled mussel, Mytilus coruscus. The peptide was purified through C18 reversed-phase high-performance liquid chromatography, and displayed antibacterial activity. Total molecular mass of 11,182 Da was determined using matrix-assisted laser desorption ionization time-of-flight mass spectrophotometry. The N-terminal 23-amino acid sequence of its purified peak was obtained through Edman degradation, revealing 82% identity with myticusin-1 of M. coruscus. Complete sequence of the target peptide was determined through cDNA cloning and rapid amplification of cDNA ends. The complete sequence comprised 574 bp with a 387-bp open reading frame (ORF) encoding 24 amino acids of a signal peptide and 104 amino acids of a mature peptide, which was named myticusin-beta. Furthermore, we discovered two novel isoforms of myticusin-beta. We constructed and expressed recombinant myticusin-beta, which displayed antimicrobial activity against gram-positive (Bacillus cereus, Bacillus subtilis, Clostridium perfringens, Staphylococcus aureus, Streptococcus iniae, Streptococcus mutans) and gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Vibrio alginolyticus, Klebsiella pneumoniae). Purified recombinant myticusin-beta also showed anti-parasitic activity at various concentrations. A short AMP analog was designed and synthesized based on the sequence of myticusin-beta, with markedly improved antimicrobial activity. Expression of myticusin-beta was detected in the mantle at the highest level, followed by hemocytes. The results obtained in this work suggest that myticusin-beta is an immune-related AMP of M. coruscus and an effective alternative to antibiotics.
•We purified 11,182 Da of a novel antimicrobial peptide from mantle tissue extract of Mytilus coruscus.•TrxA-fused recombinant myticusin-beta exhibited antibacterial and anti-scuticociliate activity without causing hemolysis.•Designed and synthesized myticusin-beta analog revealed markedly improved antimicrobial activity.•Myticusin-beta is an immune-related antimicrobial peptide of Mytilus coruscus and an effective alternative to antibiotics. |
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| AbstractList | We isolated and purified an antimicrobial peptide (AMP) from the mantle of the hard-shelled mussel, Mytilus coruscus. The peptide was purified through C18 reversed-phase high-performance liquid chromatography, and displayed antibacterial activity. Total molecular mass of 11,182 Da was determined using matrix-assisted laser desorption ionization time-of-flight mass spectrophotometry. The N-terminal 23-amino acid sequence of its purified peak was obtained through Edman degradation, revealing 82% identity with myticusin-1 of M. coruscus. Complete sequence of the target peptide was determined through cDNA cloning and rapid amplification of cDNA ends. The complete sequence comprised 574 bp with a 387-bp open reading frame (ORF) encoding 24 amino acids of a signal peptide and 104 amino acids of a mature peptide, which was named myticusin-beta. Furthermore, we discovered two novel isoforms of myticusin-beta. We constructed and expressed recombinant myticusin-beta, which displayed antimicrobial activity against gram-positive (Bacillus cereus, Bacillus subtilis, Clostridium perfringens, Staphylococcus aureus, Streptococcus iniae, Streptococcus mutans) and gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Vibrio alginolyticus, Klebsiella pneumoniae). Purified recombinant myticusin-beta also showed anti-parasitic activity at various concentrations. A short AMP analog was designed and synthesized based on the sequence of myticusin-beta, with markedly improved antimicrobial activity. Expression of myticusin-beta was detected in the mantle at the highest level, followed by hemocytes. The results obtained in this work suggest that myticusin-beta is an immune-related AMP of M. coruscus and an effective alternative to antibiotics.
•We purified 11,182 Da of a novel antimicrobial peptide from mantle tissue extract of Mytilus coruscus.•TrxA-fused recombinant myticusin-beta exhibited antibacterial and anti-scuticociliate activity without causing hemolysis.•Designed and synthesized myticusin-beta analog revealed markedly improved antimicrobial activity.•Myticusin-beta is an immune-related antimicrobial peptide of Mytilus coruscus and an effective alternative to antibiotics. We isolated and purified an antimicrobial peptide (AMP) from the mantle of the hard-shelled mussel, Mytilus coruscus. The peptide was purified through C reversed-phase high-performance liquid chromatography, and displayed antibacterial activity. Total molecular mass of 11,182 Da was determined using matrix-assisted laser desorption ionization time-of-flight mass spectrophotometry. The N-terminal 23-amino acid sequence of its purified peak was obtained through Edman degradation, revealing 82% identity with myticusin-1 of M. coruscus. Complete sequence of the target peptide was determined through cDNA cloning and rapid amplification of cDNA ends. The complete sequence comprised 574 bp with a 387-bp open reading frame (ORF) encoding 24 amino acids of a signal peptide and 104 amino acids of a mature peptide, which was named myticusin-beta. Furthermore, we discovered two novel isoforms of myticusin-beta. We constructed and expressed recombinant myticusin-beta, which displayed antimicrobial activity against gram-positive (Bacillus cereus, Bacillus subtilis, Clostridium perfringens, Staphylococcus aureus, Streptococcus iniae, Streptococcus mutans) and gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Vibrio alginolyticus, Klebsiella pneumoniae). Purified recombinant myticusin-beta also showed anti-parasitic activity at various concentrations. A short AMP analog was designed and synthesized based on the sequence of myticusin-beta, with markedly improved antimicrobial activity. Expression of myticusin-beta was detected in the mantle at the highest level, followed by hemocytes. The results obtained in this work suggest that myticusin-beta is an immune-related AMP of M. coruscus and an effective alternative to antibiotics. |
| Author | Nam, Bo-Hye Park, Jung-yeon Kim, Dong-Gyun Lee, Min Jeong Seo, Jung-Kil Kim, Young-Ok Kong, Hee Jeong Kim, Ju-Won Oh, Ryunkyoung |
| Author_xml | – sequence: 1 givenname: Ryunkyoung surname: Oh fullname: Oh, Ryunkyoung organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 2 givenname: Min Jeong surname: Lee fullname: Lee, Min Jeong organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 3 givenname: Young-Ok surname: Kim fullname: Kim, Young-Ok organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 4 givenname: Bo-Hye surname: Nam fullname: Nam, Bo-Hye organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 5 givenname: Hee Jeong surname: Kong fullname: Kong, Hee Jeong organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 6 givenname: Ju-Won surname: Kim fullname: Kim, Ju-Won organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 7 givenname: Jung-yeon surname: Park fullname: Park, Jung-yeon organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea – sequence: 8 givenname: Jung-Kil surname: Seo fullname: Seo, Jung-Kil organization: Department of Food Science and Biotechnology, Kunsan National University, Kunsan, 54150, South Korea – sequence: 9 givenname: Dong-Gyun surname: Kim fullname: Kim, Dong-Gyun email: combikola@korea.kr organization: Biotechnology Research Division, National Institute of Fisheries Science, Busan, 46083, Republic of Korea |
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| Snippet | We isolated and purified an antimicrobial peptide (AMP) from the mantle of the hard-shelled mussel, Mytilus coruscus. The peptide was purified through C18... We isolated and purified an antimicrobial peptide (AMP) from the mantle of the hard-shelled mussel, Mytilus coruscus. The peptide was purified through C... |
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| SubjectTerms | Antimicrobial peptide Myticusin-beta Mytilus coruscus Purification |
| Title | Myticusin-beta, antimicrobial peptide from the marine bivalve, Mytilus coruscus |
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