Metchnikowin

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Metchnikowin
Drosophila melanogaster Proboscis.jpg
The fruit fly, Drosophila melanogaster
Identifiers
SymbolMetchnikowin, Mtk
InterPro IPR012513

Metchnikowin is a 26-residue antimicrobial peptide of the fruit fly Drosophila melanogaster that displays both antibacterial and antifungal properties. [1] This peptide is expressed strongly in the Drosophila fat body (an organ similar to the human liver), but is also expressed at surface epithelia in the trachea and gut. This is regulated by the NF-κB signalling pathways Toll and Imd. [2] Metchnikowin is named after Russian immunologist Élie Metchnikoff, one of the founders of modern immunology.

Structure and function

Metchnikowin has microbicidal activity against the gram-negative bacterium Escherichia coli and filamentous fungus Neurospora crassa at nanomolar concentrations. [1] It is also one of the most abundant defence peptides in D. melanogaster following infection by the entomopathogenic fungus Beauveria bassiana . [3] Proline-rich peptides such as metchnikowin can bind to microbe ribosomes, preventing protein translation. [4]

Related Research Articles

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Drosophila melanogaster is a species of fly in the family Drosophilidae. The species is often referred to as the fruit fly or lesser fruit fly, however its common name is more accurately the vinegar fly. Starting with Charles W. Woodworth's proposal of the use of this species as a model organism, D. melanogaster continues to be widely used for biological research in genetics, physiology, microbial pathogenesis, and life history evolution. As of 2017, five Nobel Prizes have been awarded to [drosophilists] for their work using the animal.

Toll-like receptor

Toll-like receptors (TLRs) are a class of proteins that play a key role in the innate immune system. They are single-pass membrane-spanning receptors usually expressed on sentinel cells such as macrophages and dendritic cells, that recognize structurally conserved molecules derived from microbes. Once these microbes have breached physical barriers such as the skin or intestinal tract mucosa, they are recognized by TLRs, which activate immune cell responses. The TLRs include TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, TLR11, TLR12, and TLR13, though the last three are not found in humans, and there isn't a functional gene for TLR10 in mice. TLR1, TLR2, TLR4, TLR5, TLR6, and TLR10 are located on the cell membrane, whereas TLR3, TLR7, TLR8, and TLR9 are located in intracellular vesicles.

Defensin Group of antimicrobial peptides

Defensins are small cysteine-rich cationic proteins across cellular life, including vertebrate and invertebrate animals, plants, and fungi. They are host defense peptides, with members displaying either direct antimicrobial activity, immune signalling activities, or both. They are variously active against bacteria, fungi and many enveloped and nonenveloped viruses. They are typically 18-45 amino acids in length, with three or four highly conserved disulphide bonds.

<i>Providencia</i> (bacterium) Genus of bacteria

Providencia is genus of Gram-negative, motile bacteria of the family Morganellaceae. It was named after Providence, Rhode Island, where C. A. Stuart and colleagues studied these bacteria at Brown University.

Cathelicidin

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Jules A. Hoffmann

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Arthropod defensin

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Drosomycin

Drosomycin is an antifungal peptide from Drosophila melanogaster and was the first antifungal peptide isolated from insects. Drosomycin is induced by infection by the Toll signalling pathway, while expression in surface epithelia like the respiratory tract is instead controlled by the immune deficiency pathway (Imd). This means that drosomycin, alongside other antimicrobial peptides (AMPs) such as cecropins, diptericin, drosocin, metchnikowin and attacin, serves as a first line defence upon septic injury. However drosomycin is also expressed constitutively to a lesser extent in different tissues and throughout development.

<i>Drosophila neotestacea</i> Species of fly

Drosophila neotestacea is a member of the testacea species group of Drosophila. Testacea species are specialist fruit flies that breed on the fruiting bodies of mushrooms. These flies will choose to breed on psychoactive mushrooms such as the Fly Agaric Amanita muscaria. Drosophila neotestacea can be found in temperate regions of North America, ranging from the north eastern United States to western Canada.

Diptericin

Diptericin is a 9 kDa antimicrobial peptide (AMP) of flies first isolated from the blowfly Phormia terranova. It is primarily active against Gram-negative bacteria, disrupting bacterial membrane integrity. The structure of this protein includes a proline-rich domain with similarities to the AMPs drosocin, pyrrhocoricin, and abaecin, and a glycine-rich domain with similarity to attacin. Diptericin is an iconic readout of immune system activity in flies, used ubiquitously in studies of Drosophila immunity. Diptericin is named after the insect order Diptera.

Drosocin Antimicrobial peptide

Drosocin is a 19-residue long antimicrobial peptide (AMP) of flies first isolated in the fruit fly Drosophila melanogaster, and later shown to be conserved throughout the genus Drosophila. Drosocin is regulated by the NF-κB Imd signalling pathway in the fly.

Pyrrhocoricin Peptide

Pyrrhocoricin is a 20-residue long antimicrobial peptide of the firebug Pyrrhocoris apterus.

<i>Drosophila quinaria</i> species group Species group of the subgenus Drosophila

The Drosophila quinaria species group is a speciose lineage of mushroom-feeding flies studied for their specialist ecology, their parasites, population genetics, and the evolution of immune systems. Quinaria species are part of the Drosophila subgenus.

<i>Drosophila innubila</i> Species of fly

Drosophila innubila is a species of vinegar fly restricted to high-elevation woodlands in the mountains of the southern USA and Mexico, which it likely colonized during the last glacial period. Drosophila innubila is a kind of mushroom-breeding Drosophila, and member of the Drosophila quinaria species group. Drosophila innubila is best known for its association with a strain of male-killing Wolbachia bacteria. These bacteria are parasitic, as they drain resources from the host and cause half the infected female's eggs to abort. However Wolbachia may offer benefits to the fly's fitness in certain circumstances. The D. innubila genome was sequenced in 2019.

Imd pathway Immune signaling pathway of insects

The Imd pathway is a broadly-conserved NF-κB immune signalling pathway of insects and some arthropods that regulates a potent antibacterial defence response. The pathway is named after the discovery of a mutation causing severe immune deficiency. The Imd pathway was first discovered in 1995 using Drosophila fruit flies by Bruno Lemaitre and colleagues, who also later discovered that the Drosophila Toll gene regulated defence against Gram-positive bacteria and fungi. Together the Toll and Imd pathways have formed a paradigm of insect immune signalling; as of September 2, 2019, these two landmark discovery papers have been cited collectively over 5000 times since publication on Google Scholar.

Bruno Lemaitre French immunologist

Bruno Lemaitre is a French immunologist and a professor at the École Polytechnique Fédérale de Lausanne (EPFL). His research focuses on the mechanisms of innate immunity and endosymbiosis in Drosophila. Lemaitre has also authored several books on the topic of narcissism in science.

References

  1. 1 2 Levashina EA, Ohresser S, Bulet P, Reichhart JM, Hetru C, Hoffmann JA (October 1995). "Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties". European Journal of Biochemistry. 233 (2): 694–700. doi: 10.1111/j.1432-1033.1995.694_2.x . PMID   7588819.
  2. Levashina EA, Ohresser S, Lemaitre B, Imler JL (May 1998). "Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin". Journal of Molecular Biology. 278 (3): 515–27. doi:10.1006/jmbi.1998.1705. PMID   9600835.
  3. Lemaitre B, Reichhart JM, Hoffmann JA (December 1997). "Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms". Proceedings of the National Academy of Sciences of the United States of America. 94 (26): 14614–9. Bibcode:1997PNAS...9414614L. doi: 10.1073/pnas.94.26.14614 . PMC   25070 . PMID   9405661.
  4. Florin T, Maracci C, Graf M, Karki P, Klepacki D, Berninghausen O, Beckmann R, Vázquez-Laslop N, Wilson DN, Rodnina MV, Mankin AS (September 2017). "An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome". Nature Structural & Molecular Biology. 24 (9): 752–757. doi:10.1038/nsmb.3439. PMC   5589491 . PMID   28741611.