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Updated: Nov 2, 2025

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
The proline-rich myticalins from Mytilus galloprovincialis display a membrane-permeabilizing antimicrobial mode of
Sabrina Pacor1, Monica Benincasa1, Maria Valentina Musso1
1Department of Life Sciences, Via Licio Giorgieri 5, University of Trieste, 34127 Trieste, Italy.
Abstract:
Bivalve mollusks are continuously exposed to potentially pathogenic microorganisms living in the marine environment. Not surprisingly, these filter-feeders developed a robust innate immunity to protect themselves, which includes a broad panel of antimicrobial peptides. Among these, myticalins represent a recently discovered family of linear cationic peptides expressed in the gills of Mytilus galloprovincialis. Even though myticalins and insect and mammalian proline-rich antimicrobial peptides (PrAMPs) share a similar amino acid composition, we here show that none of the tested mussel peptides use a non-lytic mode of action relying on the bacterial transporter SbmA. On the other hand, all the tested myticalins perturbed and permeabilized the membranes of E. coli BW25113, as shown by flow-cytometry and atomic force microscopy. Circular dichroism spectra revealed that most myticalins did not adopt recognizable secondary structures in the presence of amphipathic environments, such as biological membranes. To explore possible uses of myticalins for biotech, we assessed their biocompatibility with a human cell line. Non-negligible cytotoxic effects displayed by myticalins indicate that their optimization would be required before their further use as lead compounds in the development of new antibiotics.
Insights
Mussel antimicrobial peptides called myticalins damage bacterial membranes but do not rely on the SbmA transporter. Further research is needed to optimize myticalins for potential antibiotic development due to cytotoxicity concerns.
Area of Science:
- Marine biology
- Immunology
- Biochemistry
Background:
- Bivalve mollusks face constant exposure to marine pathogens.
- They possess innate immunity, including antimicrobial peptides, for defense.
- Myticalins are a novel family of linear cationic peptides found in Mytilus galloprovincialis gills.
Purpose of the Study:
- Investigate the mechanism of action of myticalins.
- Compare myticalin function to proline-rich antimicrobial peptides (PrAMPs).
- Assess myticalin biocompatibility for potential biotechnological applications.
Main Methods:
- Tested myticalin interaction with the bacterial transporter SbmA.
- Utilized flow cytometry and atomic force microscopy to assess membrane perturbation and permeabilization in E. coli.
- Employed circular dichroism spectroscopy to analyze peptide secondary structures in membrane-mimicking environments.
- Evaluated myticalin cytotoxicity against a human cell line.
Main Results:
- Myticalins did not utilize the SbmA transporter, unlike some PrAMPs.
- All tested myticalins effectively perturbed and permeabilized E. coli membranes.
- Most myticalins showed limited stable secondary structures in amphipathic environments.
- Myticalins exhibited significant cytotoxic effects on a human cell line.
Conclusions:
- Myticalins possess a distinct membrane-disrupting antimicrobial mechanism.
- Their mode of action differs from SbmA-dependent PrAMPs.
- Cytotoxicity necessitates optimization for future antibiotic development.
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