Journal
FISH & SHELLFISH IMMUNOLOGY
Volume 131, Issue -, Pages 817-826Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fsi.2022.10.057
Keywords
Mytilus coruscus; Antimicrobial peptide; Myticofensin; Expression profile; Chemical synthesis
Funding
- National Natural Science Foundation of China [42020104009, 41976111, 42176099]
- Science Foundation of Donghai Laboratory [DH- 2022KF0219]
- Project of Education of Zhejiang province [Y202044838]
- Project of Zhoushan Science and Technology Bureau [2019F12004]
- Program of Scientific and Techno- logical Innovation (Xinmiao Talents Program) of Zhejiang Province [2020R411050]
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A novel AMP family called myticofensins, similar to arthropod defensins, was identified in Mytilus coruscus. These myticofensins showed high expression levels in immune-related tissues and their expression could be significantly increased under microbial challenges. Different myticofensins may have different immune functions in different tissues.
In this study, seven transcripts representing a novel antimicrobial peptide (AMP) family with structural features similar to those of arthropod defensins were identified from Mytilus coruscus. These novel defensins from the Mytilus AMP family were named myticofensins. To explore the possible immune-related functions of these myticofensins, we examined their expression profiles in different tissues and larval stages, as well as in three immune-related tissues under the threat of different microbes. Our data revealed that the seven myticofensins had relatively high expression levels in immune-related tissues. Most myticofensins were undetectable, or had low expression levels, in different larval mussel stages. Additionally, in vivo microbial challenges significantly increased the expression levels of myticofensins in M. coruscus hemocytes, gills, and digestive glands, showing different immune response patterns under challenges from different microbes. Our data indicates that different myticofensins may have different immune functions in different tissues. Furthermore, peptide sequences corresponding to the beta-hairpin, alpha-helix, and N-terminal loop of myticofensin were synthesized and the antimicrobial activities of these peptide fragments were tested. Our data confirms the diversity of defensins in Mytilus and reports the complex regulation of these defensins in the mussel immune response to different microbes in immune-related tissues. The immune system of Mytilus has been studied for years as they are a species with strong environmental adaptations. Our data can be regarded as a step forward in the study of the adaptation of Mytilus spp. to an evolving microbial world.
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