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

B. Mason, I. Cooke, A. Moya, R. Augustin, M. F. Lin, N. Satoh, T. C.G. Bosch, D. G. Bourne, D. C. Hayward, N. Andrade, S. Forêt, H. Ying, E. E. Ball*, D. J. Miller*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    11 Citations (Scopus)

    Abstract

    A candidate antimicrobial peptide (AmAMP1) was identified by searching the whole genome sequence of Acropora millepora for short (<125AA) cysteine-rich predicted proteins with an N-terminal signal peptide but lacking clear homologs in the SwissProt database. It resembled but was not closely related to damicornin, the only other known AMP from a coral, and was shown to be active against both Gram-negative and Gram-positive bacteria. These proteins define a family of AMPs present in corals and their close relatives, the Corallimorpharia, and are synthesised as preproproteins in which the C-terminal mature peptide contains a conserved arrangement of six cysteine residues. Consistent with the idea of a common origin for AMPs and toxins, this Cys motif is shared between the coral AMPs and the Shk neurotoxins of sea anemones. AmAMP1 is expressed at late stages of coral development, in ectodermal cells that resemble the “ganglion neurons” of Hydra, in which it has recently been demonstrated that a distinct AMP known as NDA-1 is expressed.

    Original languageEnglish
    Article number103866
    JournalDevelopmental and Comparative Immunology
    Volume114
    DOIs
    Publication statusPublished - Jan 2021

    Fingerprint

    Dive into the research topics of 'AmAMP1 from Acropora millepora and damicornin define a family of coral-specific antimicrobial peptides related to the Shk toxins of sea anemones'. Together they form a unique fingerprint.

    Cite this