User:Bzetko/Myticin
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Myticin is a cysteine-rich peptide produced in three isoforms, A, B and C, by Mytilus galloprovincialis (Mediterranean mussel). Myticin is also produced in other species of Mytilus (Mytilus spp.), though the properties of Myticin in Mytilus galloprovincialis is understood to a greater extent. [1]Isoforms A and B show antibacterial activity against Gram-positive bacteria, while isoform C is additionally active against the fungus Fusarium oxysporum[2] and bacterium Escherichia coli (streptomycin resistant strain D31). Isoform C has also been shown to have antiviral properties against OsHV-1, which is one of the most important and devastating bivalve pathogens. [3] Myticin-prepro is the precursor peptide.[edit]
The mature molecule, named myticin, consists of 40 residues, with four intramolecular disulphide bridges, an N-terminal signal peptide,[4] and a cysteine array in the primary structure different from that of previously characterized cysteine-rich antimicrobial peptides. The first 20 amino acids are a putative signal peptide, and the antimicrobial peptide sequence is a 36-residue C-terminal extension. Such a structure suggests that myticins are synthesized as prepro-proteins that are then processed by various proteolytic events before storage in the hemocytes as the active peptide. Myticin precursors are expressed mainly in the hemocytes.
The Role of Myticin in Mytilus galloprovincialis[edit]
AMPs (Antimicrobial peptides) play a significant role in innate immunity defenses exhibited by Bivalves. In marine organisms, AMPs are the main factor in innate immune response which helps to protect them against pathogenic microorganisms in their environment.[5] The innate immune response is thought be nonspecific, though there is limited research in this area. [6] Myticin is expressed in the hemocytes of mussels, and recent studies have suggested that this molecule is activated after injury to its tissues. [7]
Myticin: Isoform C[edit]
Isoform C is the most widely studied isoform of myticin, most likely due to it's abundance and diversity. Myticin C has shown a wide diversity in Mytilus galloprovincialis, with individuals expressing unique sequences of the peptide compared to genes that were not immune related. [8] It has been shown to be an active defense mechanism against many organisms including fish rhabdovirus. [9]
References[edit]
- ^ Yang, Jinyue; He, Jianyu; Liu, Lu; He, Menglan; Zhang, Xiaolin; Buttino, Isabella; Guo, Baoying; Yan, Xiaojun; Liao, Zhi (2022-02-15). "Expression profiles of antimicrobial peptides in Mytilus coruscus". Aquaculture. 548: 737709. doi:10.1016/j.aquaculture.2021.737709. ISSN 0044-8486.
- ^ Mitta, Guillaume; Hubert, Florence; Noel, Thierry; Roch, Philippe (1999-10). "Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis". European Journal of Biochemistry. 265 (1): 71–78. doi:10.1046/j.1432-1327.1999.00654.x. ISSN 0014-2956.
{{cite journal}}: Check date values in:|date=(help) - ^ Novoa, Beatriz; Romero, Alejandro; Álvarez, Ángel L.; Moreira, Rebeca; Pereiro, Patricia; Costa, María M.; Dios, Sonia; Estepa, Amparo; Parra, Francisco; Figueras, Antonio (2016-09). Jung, J. U. (ed.). "Antiviral Activity of Myticin C Peptide from Mussel: an Ancient Defense against Herpesviruses". Journal of Virology. 90 (17): 7692–7702. doi:10.1128/JVI.00591-16. ISSN 0022-538X. PMC 4988142. PMID 27307570.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: PMC format (link) - ^ Padhi, Abinash; Verghese, Bindhu (2008-07-01). "Molecular diversity and evolution of myticin-C antimicrobial peptide variants in the Mediterranean mussel, Mytilus galloprovincialis". Peptides. 29 (7): 1094–1101. doi:10.1016/j.peptides.2008.03.007. ISSN 0196-9781.
- ^ Balseiro, Pablo; Falcó, Alberto; Romero, Alejandro; Dios, Sonia; Martínez-López, Alicia; Figueras, Antonio; Estepa, Amparo; Novoa, Beatriz (2011-08-08). "Mytilus galloprovincialis Myticin C: A Chemotactic Molecule with Antiviral Activity and Immunoregulatory Properties". PLOS ONE. 6 (8): e23140. doi:10.1371/journal.pone.0023140. ISSN 1932-6203. PMC 3152575. PMID 21858010.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link) - ^ Watson, Angus; Agius, Jacinta; Ackerly, Danielle; Beddoe, Travis; Helbig, Karla (2022-03). "The Role of Anti-Viral Effector Molecules in Mollusc Hemolymph". Biomolecules. 12 (3): 345. doi:10.3390/biom12030345. ISSN 2218-273X.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: unflagged free DOI (link) - ^ Rey-Campos, Magalí; Moreira, Rebeca; Romero, Alejandro; Medina-Gali, Regla M.; Novoa, Beatriz; Gasset, María; Figueras, Antonio (2020-01). "Transcriptomic Analysis Reveals the Wound Healing Activity of Mussel Myticin C". Biomolecules. 10 (1): 133. doi:10.3390/biom10010133. ISSN 2218-273X.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: unflagged free DOI (link) - ^ Costa, M. M.; Dios, S.; Alonso-Gutierrez, J.; Romero, A.; Novoa, B.; Figueras, A. (2009-02-01). "Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis)". Developmental & Comparative Immunology. 33 (2): 162–170. doi:10.1016/j.dci.2008.08.005. ISSN 0145-305X.
- ^ Martinez-Lopez, Alicia; Encinar, Jose Antonio; Medina-Gali, Regla Maria; Balseiro, Pablo; Garcia-Valtanen, Pablo; Figueras, Antonio; Novoa, Beatriz; Estepa, Amparo (2013-07). "pH-Dependent Solution Structure and Activity of a Reduced Form of the Host-Defense Peptide Myticin C (Myt C) from the Mussel Mytilus galloprovincialis". Marine Drugs. 11 (7): 2328–2346. doi:10.3390/md11072328. ISSN 1660-3397.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: unflagged free DOI (link)