Baramicin

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Baramicin
Identifiers
Organism Drosophila melanogaster
SymbolBara
UniProt C0HLZ9
Search for
Structures Swiss-model
Domains InterPro

Baramicin (Bara) is an antimicrobial peptide gene of the fruit fly Drosophila melanogaster . Baramicin is a prominent element of the fly immune response: of the most abundant immune peptides detected in the fly hemolymph, the BaraA gene is responsible for 9 of the 24 peptides first described for their high concentrations after systemic infection. [1] [2] [3]

Contents

Etymology

The name of the Baramicin gene was inspired by One Piece character “Buggy" and derives from the Japanese expression "Bara Bara", an onomatopoeia for things breaking apart, in reference to the Baramicin precursor breaking into multiple sub-peptides. [3]

Activity

The Baramicin A precursor protein can be broken into three distinct domains: the IM10-like, IM22, and IM24 domains. Five sub-peptides are produced by the BaraA precursor including one IM24 peptide, three IM10-like peptides, and one IM22 peptide. [3]

Immune response

The Baramicin gene is part of the Toll pathway antifungal immune response. [1] [2] Flies lacking BaraA genetically are susceptible to infection by entomopathogenic fungi such as Beauveria bassiana and Metarhizium species, but also show some susceptibility to Enterococcus faecalis bacterial infection. [3] [4] The IM10-like peptides of BaraA are specifically proposed as antifungal peptides produced by the BaraA gene. [3] The potential activity of the IM22 and IM24 peptides is unknown. Some element of the Baramicin protein may also regulate a behavioural response after infection, as flies lacking Baramicin display an erect wing phenotype after immune activation. [3]

Nervous system

Antimicrobial peptides and neuropeptides share many common features. [5] The distinction between which of these two roles, if either, is the primary function of any given peptide is often unclear. [6] [7] The Baramicin gene family of D. melanogaster includes the immune-induced BaraA and also two non-immune Baramicin genes BaraB and BaraC. The BaraB and BaraC genes are expressed in the nervous system, in neurons or glia respectively. Evolutionary study suggests the IM24 domain is the key element of the Baramicin precursor that is involved in Baramicin function in the nervous system. This finding suggests antimicrobial peptides and neuropeptides might accomplish immune or neural roles not only by dual action of a single peptide, but rather by different mechanisms of action of sub-peptides. [8]

BaraA mutants also display a reduced recovery rate after the injection of neurotoxins, which is rescued somewhat by expressing BaraA in glial cells of the fly's nervous system. [4] Together with the description of antifungal activity of IM10-like peptides, [3] the BaraA gene therefore encodes both immune antimicrobials and some factor that promotes host resilience in the face of microbial toxins. [4]

Related Research Articles

<i>Drosophila melanogaster</i> Species of fruit fly

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, or less commonly the "vinegar fly", "pomace fly", or "banana fly". Starting with Charles W. Woodworth's 1901 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, six Nobel Prizes have been awarded to drosophilists for their work using the insect.

<span class="mw-page-title-main">Toll-like receptor</span> Pain receptors and inflammation

Toll-like receptors (TLRs) are a class of proteins that play a key role in the innate immune system. They are single-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 reached 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. Humans lack genes for TLR11, TLR12 and TLR13 and mice lack a functional gene for TLR10. The receptors TLR1, TLR2, TLR4, TLR5, TLR6, and TLR10 are located on the cell membrane, whereas TLR3, TLR7, TLR8, and TLR9 are located in intracellular vesicles.

<span class="mw-page-title-main">Neuropeptide</span> Peptides released by neurons as intercellular messengers

Neuropeptides are chemical messengers made up of small chains of amino acids that are synthesized and released by neurons. Neuropeptides typically bind to G protein-coupled receptors (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart.

β-Endorphin Peptide hormone in humans

β-Endorphin (beta-endorphin) is an endogenous opioid neuropeptide and peptide hormone that is produced in certain neurons within the central nervous system and peripheral nervous system. It is one of three endorphins that are produced in humans, the others of which include α-endorphin and γ-endorphin.

<span class="mw-page-title-main">Cathelicidin</span> Group of antimicrobial peptides in vertebrates

Cathelicidin antimicrobial peptide (CAMP) is a polypeptide that is primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs); in humans, the CAMP gene encodes the peptide precursor CAP-18, which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37. LL-37 is the only peptide in the Cathelicidin family found in the human body.

<span class="mw-page-title-main">Jules A. Hoffmann</span> French biologist

Jules Alphonse Nicolas Hoffmann is a Luxembourg-born French biologist. During his youth, growing up in Luxembourg, he developed a strong interest in insects under the influence of his father, Jos Hoffmann. This eventually resulted in the younger Hoffmann's dedication to the field of biology using insects as model organisms. He currently holds a faculty position at the University of Strasbourg. He is a research director and member of the board of administrators of the National Center of Scientific Research (CNRS) in Strasbourg, France. He was elected to the positions of Vice-President (2005-2006) and President (2007-2008) of the French Academy of Sciences. Hoffmann and Bruce Beutler were jointly awarded a half share of the 2011 Nobel Prize in Physiology or Medicine for "their discoveries concerning the activation of innate immunity,". [More specifically, the work showing increased Drosomycin expression following activation of Toll pathway in microbial infection.]

<span class="mw-page-title-main">Arthropod defensin</span>

Arthropod defensins are a family defensin proteins found in mollusks, insects, and arachnids. These cysteine-rich antibacterial peptides are primarily active against Gram-positive bacteria and fungi in vitro. However Drosophila fruit flies mutant for the fly defensin were more susceptible to infection by the Gram-negative bacteria Providencia burhodogranariea, and resisted infection against Gram-positive bacteria like wild-type flies. It remains to be seen how in vitro activity relates to in vivo function. Mutants for the defensin-like antimicrobial peptide Drosomycin were more susceptible to fungi, validating a role for defensin-like peptides in anti-fungal defence.

Lingual antimicrobial peptide (LAP) is a beta-defensin found in bovine internal epithelial tissue, in particular, that of the digestive tract. It has antimicrobial activity against many different pathogens. It was first isolated from an inflamed cattle tongue, hence its designation as lingual. Since then it has been found more extensively throughout the body; its presence has even been detected in bovine milk. Its expression is selective and increases in inflamed areas. LAP may have a closer relationship with immune response than simple antimicrobial activity, such as an association with growth factor activity.

The microbiota are the sum of all symbiotic microorganisms living on or in an organism. The fruit fly Drosophila melanogaster is a model organism and known as one of the most investigated organisms worldwide. The microbiota in flies is less complex than that found in humans. It still has an influence on the fitness of the fly, and it affects different life-history characteristics such as lifespan, resistance against pathogens (immunity) and metabolic processes (digestion). Considering the comprehensive toolkit available for research in Drosophila, analysis of its microbiome could enhance our understanding of similar processes in other types of host-microbiota interactions, including those involving humans. Microbiota plays key roles in the intestinal immune and metabolic responses via their fermentation product, acetate.

<span class="mw-page-title-main">Drosomycin</span>

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.

<span class="mw-page-title-main">Diptericin</span>

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.

<span class="mw-page-title-main">Drosocin</span> 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.

<span class="mw-page-title-main">Metchnikowin</span> Antimicrobial peptide

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

<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.

<span class="mw-page-title-main">Imd pathway</span> 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.

<span class="mw-page-title-main">Bruno Lemaitre</span> 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. and a book on the philosophy of Michael Polanyi.

<span class="mw-page-title-main">Bomanin</span> Antimicrobial peptide-like immune gene of fruit flies

The Bomanin gene family encodes a group of immune peptides that are essential for Drosophila fruit fly defence against infection by many pathogens.

Daisho (<i>Drosophila</i> peptide) Antimicrobial peptide immune gene of fruit flies

Daisho (Dso) is an antimicrobial peptide gene family of the fruit fly Drosophila melanogaster. Two Daisho genes are encoded in tandem in the fruit fly genome, one shorter than the other. This pair of genes with different length was named "Daisho" in reference to Daisho Japanese swords, which come in pairs with one shorter than the other.

References

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Further reading