AmAMP1 from Acropora millepora and damicornin define a family of coral-specific antimicrobial peptides related to the Shk toxins of sea anemones

Ribosomally synthesized peptides, foreground players in microbial interactions: recent developments and unanswered questions

“…Recently a second antimicrobial URiP sharing common characteristics with damicornin was characterized in the coral Acropora millepora (Acroporidae) and confirmed the commonality between these coral defence peptides and toxins from sea anemones. 207…”

Embracing the era of antimicrobial peptides with marine organisms

“…AmAMP1 from coral Acropora millepora has a signal peptide and the mature peptide shares no homology to other identified or predicted AMPs, suggesting it could be a coral-specific AMP family. 66 In the sea anemone, a β-Defensin-like peptide and a magnificamide, were determined from the Heteractis magnifica . Several novel AMPs were identified from the transcriptome of sea anemone Cnidopus japonicus , and peptide A3, B1, and B4 with 15, 10, and 10 residues respectively showed the most potent antimicrobial activities.…”

Marine natural products

“…593 Genome mining of the branching stony coral Acropora millepora identied a predicted protein sequence AmAMP1 that shared some resemblance to known coral and jellysh antimicrobial peptides and for which homologues could be identied in a range of other corals. 594 The mature peptide contains six cysteine residues making it related to the Shk group of sea anemone neurotoxins. Synthesised peptides derived from the protein sequence demonstrated activity towards both Grampositive and Gram-negative bacteria.…”