Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia)
The CS-αβ architecture is a structural scaffold shared by a high number of small, cationic, cysteine-rich defense peptides, found in nearly all the major branches of the tree of life. Although several CS-αβ peptides involved in innate immune response have been des...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-01-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/9/1/37 |
| _version_ | 1818265605514461184 |
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| author | Samuele Greco Marco Gerdol Paolo Edomi Alberto Pallavicini |
| author_facet | Samuele Greco Marco Gerdol Paolo Edomi Alberto Pallavicini |
| author_sort | Samuele Greco |
| collection | DOAJ |
| description | The CS-αβ architecture is a structural scaffold shared by a high number of small, cationic, cysteine-rich defense peptides, found in nearly all the major branches of the tree of life. Although several CS-αβ peptides involved in innate immune response have been described so far in bivalve mollusks, a clear-cut definition of their molecular diversity is still lacking, leaving the evolutionary relationship among defensins, mytilins, myticins and other structurally similar antimicrobial peptides still unclear. In this study, we performed a comprehensive bioinformatic screening of the genomes and transcriptomes available for marine mussels (Mytilida), redefining the distribution of mytilin-like CS-αβ peptides, which in spite of limited primary sequence similarity maintain in all cases a well-conserved backbone, stabilized by four disulfide bonds. Variations in the size of the alpha-helix and the two antiparallel beta strand region, as well as the positioning of the cysteine residues involved in the formation of the C1−C5 disulfide bond might allow a certain degree of structural flexibility, whose functional implications remain to be investigated. The identification of mytilins in <i>Trichomya</i> and <i>Perna</i> spp. revealed that many additional CS-αβ AMPs remain to be formally described and functionally characterized in Mytilidae, and suggest that a more robust scheme should be used for the future classification of such peptides with respect with their evolutionary origin. |
| first_indexed | 2024-12-12T19:53:28Z |
| format | Article |
| id | doaj.art-290cd3739b3a471ebf31cbd9fb4a7224 |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-12-12T19:53:28Z |
| publishDate | 2020-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-290cd3739b3a471ebf31cbd9fb4a72242022-12-22T00:13:56ZengMDPI AGAntibiotics2079-63822020-01-01913710.3390/antibiotics9010037antibiotics9010037Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia)Samuele Greco0Marco Gerdol1Paolo Edomi2Alberto Pallavicini3Department of Life Sciences, University of Trieste, 34127 Trieste, ItalyDepartment of Life Sciences, University of Trieste, 34127 Trieste, ItalyDepartment of Life Sciences, University of Trieste, 34127 Trieste, ItalyDepartment of Life Sciences, University of Trieste, 34127 Trieste, ItalyThe CS-αβ architecture is a structural scaffold shared by a high number of small, cationic, cysteine-rich defense peptides, found in nearly all the major branches of the tree of life. Although several CS-αβ peptides involved in innate immune response have been described so far in bivalve mollusks, a clear-cut definition of their molecular diversity is still lacking, leaving the evolutionary relationship among defensins, mytilins, myticins and other structurally similar antimicrobial peptides still unclear. In this study, we performed a comprehensive bioinformatic screening of the genomes and transcriptomes available for marine mussels (Mytilida), redefining the distribution of mytilin-like CS-αβ peptides, which in spite of limited primary sequence similarity maintain in all cases a well-conserved backbone, stabilized by four disulfide bonds. Variations in the size of the alpha-helix and the two antiparallel beta strand region, as well as the positioning of the cysteine residues involved in the formation of the C1−C5 disulfide bond might allow a certain degree of structural flexibility, whose functional implications remain to be investigated. The identification of mytilins in <i>Trichomya</i> and <i>Perna</i> spp. revealed that many additional CS-αβ AMPs remain to be formally described and functionally characterized in Mytilidae, and suggest that a more robust scheme should be used for the future classification of such peptides with respect with their evolutionary origin.https://www.mdpi.com/2079-6382/9/1/37bivalvesmusselsantimicrobial peptidesinnate immunitydefensins |
| spellingShingle | Samuele Greco Marco Gerdol Paolo Edomi Alberto Pallavicini Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia) Antibiotics bivalves mussels antimicrobial peptides innate immunity defensins |
| title | Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia) |
| title_full | Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia) |
| title_fullStr | Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia) |
| title_full_unstemmed | Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia) |
| title_short | Molecular Diversity of Mytilin-Like Defense Peptides in Mytilidae (Mollusca, Bivalvia) |
| title_sort | molecular diversity of mytilin like defense peptides in mytilidae mollusca bivalvia |
| topic | bivalves mussels antimicrobial peptides innate immunity defensins |
| url | https://www.mdpi.com/2079-6382/9/1/37 |
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