Ann N Y Acad Sci 2012 Oct 01;1270:79-85. doi: 10.1111/j.1749-6632.2012.06652.x.

Fragments of β-thymosin from the sea urchin Paracentrotus lividus as potential antimicrobial peptides against staphylococcal biofilms.

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The immune mediators in echinoderms can be a potential source of novel antimicrobial peptides (AMPs) applied toward controlling pathogenic staphylococcal biofilms that are intrinsically resistant to conventional antibiotics. The peptide fraction <5 kDa from the cytosol of coelomocytes of the sea urchin Paracentrotus lividus (5-CC) was tested against a group of Gram-positive and Gram-negative pathogen reference strains. The 5-CC of P. lividus was active against all planktonic-tested strains but also showed antibiofilm properties against staphylococcal strains. Additionally, we demonstrated the presence of three small peptides in the 5-CC belonging to segment 9-41 of a P. lividusβ-thymosin. The smallest of these peptides in particular, showed the common chemical-physical characteristics of AMPs. This novel AMP from β-thymosin has high potential activity as an antibiofilm agent, acting on slow-growing bacterial cells that exhibit a reduced susceptibility to conventional antibiotics and represent a reservoir for recurrent biofilm-associated infections.

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Genes referenced: LOC100887844 LOC373484