D S A DInsect Antimicrobial Peptides D Therapeutic And Agriculture .
Journal of1-J Appl Biotechnol Rep. 2021 September;8(3):193-202doi 10.30491/JABR.2020.236075.1242DSADDASDHabeebShaik Mohideen 1* , Henry Pearl Louis 1Applied BiotechnologyReportsReview ArticleInsect Antimicrobial Peptides – Therapeutic and AgriculturePerspective1 Bioinformatics& Entomoinformatics Lab, Department of Genetic Engineering, SRM Institute of Science & Technology, Kattankulathur,Tamilnadu–603202, IndiaCorresponding Author: Habeeb Shaik Mohideen, PhD, Associate Professor, Bioinformatics & Entomoinformatics Lab, Departmentof Genetic Engineering, SRM Institute of Science & Technology, Kattankulathur, Tamilnadu–603202, India. Tel: 91-9940051100,E-mail: Habeeb skm@yahoo.co.in, habeebm@srmist.edu.inReceived June 21, 2020; Accepted November 3, 2020; Online Published April 25, 2021AbstractAntimicrobial resistance (AMR) has become a menace for humanity. Several antibiotics have become ineffective, and there is a need for a novelroute or approach to find solutions. Antimicrobial peptides (AMPs) have already generated a lot of noise for over four decades. However, insectbased AMPs offer not only novel sources but also provide effective measures, as the insects are known to be exposed to extreme environments.Plenty of insect-based AMPs have been identified from different orders of insect taxonomy. This review concentrates on the world of insectbased AMPs, their known targets and their applications in agriculture and medical fields. Transgenic induction of AMPs in different hosts hasbeen successfully studied in plant systems. By identifying new AMPs, it will also help in the field of agriculture to increase the production rate ofthe crops by eliminating the disease-causing pathogens, microbes, and pests. In the present review, we have discussed recent knowledge, andseveral essential medical and agricultural importance of AMPs identified from insects.Keywords: Insect, Antimicrobial Peptides, Antimicrobial Resistance, High Throughput Screening, Plant-microbe Interaction, Crop ProtectionCitation: Mohideen HS, Louis HP. Insect Antimicrobial Peptides–Therapeutic and Agriculture Perspective. J Appl Biotechnol Rep. 2021;8(3):193-202. microbial resistance (AMR) has become a universalthreat, rendering antibiotics ineffective and useless, therebyresulting in severely infected individuals and highermortality rates.1 The World Health Organization (WHO)predicted the need for innovative solutions against the AMRnearly two decades ago.2 The menace is so disturbing thatseveral hundred thousand deaths are being recorded everyyear across the world due to AMR.3 These are reported frompost-operative/transplantation procedures, neonatal intensivecare,4 failed chemotherapy,5 replacement surgeries etc.Annually, AMR is estimated to enforce the loss of about 9billion 6 in Europe and 20 billion in the USA.3 Due to thesereasons, it is imperative to find solutions for better controlthat is not only viable but also has a broad-spectrum effectwith less or no side effects.7Antimicrobial peptides (AMPs) are peptide-based effectormolecules that are discovered for the treatment of varioushuman diseases. AMPs are mostly formed naturally by thehost innate immune system of all the organisms.8,9 One ofthe first AMP was reported in 1947 from Lactococcus lactis.10Thousands of AMPs have been reported from differentforms of life mainly the eukaryotes such as plants, animals,and fungi. The AMPs act as the first line of defense in theseorganisms and have a unique potential to attack microbes,including the resistant ones11The AMPs that are being used universally have similarcharacteristics. For example, they are cationic (net vecharge 2 to 9) and amphipathic. Certain factors likehydrophobicity, a combination of charge and peptide length,are essential for their antimicrobial property, whereas anychange in peptide chain position will affect theirfundamental secondary structure.12,13 According to Boman’sclassification of antimicrobial peptides, they are differentiatedinto four families based on their secondary structures. Theyare (a) α-helical structure due to coiled conformation, (b) βsheet or stranded, (c) both α-helix /β-stranded mixed, and (d)extended chains respectively.14Naturally, these AMPs consist of about 12 – 50 amino acidresidues and based on their structure and composition, aredivided into several subgroups. Some AMPs are longer in astructure consisting of 100 amino acid residues. Further,AMPs from eukaryotes can be categorized into cationic andalso some anionic peptides like Maximin and Dermcidin.More than 3050 AMPs have been discovered from variousspecies, such as bacteria, fungi, plants, and also animals.These peptides will be a stable alternative for antibioticsCopyright 2021 The Author(s). This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properlycited.
Insect Antimicrobial Peptidesused traditionally based on easy concepts of modificationand extraction. Recent developments in the field of bioinformaticsand biotechnology have made it possible for AMP identification/synthesis. Novel AMPs have been discovered based on thepeptide homology by identifying the presence of proteasecleavage sites and focusing on high immune resistant tissuesand cells by their expression profiles.15,16 In general, basedon the experimental evidence, these peptides disrupt the cellmembrane of microorganisms through different mechanisms.Most studies shown that disrupting the integrity of the cellmembrane is the main mechanism of action of these peptidesfor killing microorganisms (Figure 1).Mostly identified AMPs are inactive precursor proteinsgenerated by low proteolysis level known as active peptides(20-50 residues). In fruit fly, about seven classes of AMPshave been identified till now, and gene regulation of thoseidentified AMPs have been well studied for betterunderstanding.17,18 Although many insect AMPs have beenreported from recent research, there are only a few reviewsabout them.Insect Antimicrobial PeptidesGlobally, about 10 quintillion insects are estimated, and thelargest group of insect families are Beetles, which compriseabout 350,000 to 400,000 species.19 While comparing withother species, insects are potential sources of various proteins,fats, and some other essential nutrients.20 Insects habituatingin densely populated regions are likely more resistant tovarious infectious pathogens when compared to low populationdensity, and this may also affect host-pathogen interactionstability.19,21 It is all about the threats faced by an individualspecies in the environment to survive from the pathogensduring the evolution. For example, when the species getshighly exposed to the pathogenic environment with varioustypes of them, it is expected that the species will produce amore qualitative and quantitative amount of defensive moleculesor macromolecules like AMPs.18,22The insect innate immune response mainly consists ofhumoral immunity and cellular immunity. The advantage isa broad spectrum of combat, and they physically disruptmicrobial cell membranes, which are considered as theprimary target of AMPs. The AMPs eliminate microorganismslike bacteria and fungi by the formation of transmembranepores or ion channels, then showing the unique characteristicsof killing other viruses and protozoa. They can bind andneutralize endotoxins and then regulate the immuneresponses. They also affect several processes together in thepathogens such as synthesis of the membrane and fatty acid,regulation of membrane, and chemotaxis.23 AMPs also showproperties like the Antineoplastic effect, healing of wounds,and skin regeneration. They have also shown cytotoxiceffects on Leukemia, Mouse myeloma, Lymphoma, Lungcancer, Breast cancer, etc.24-27Recently, these AMPs have also been identified more innumbers from transcriptomes of insects. Therefore,transcriptomic profiling provided various types of insectbased AMPs, namely, Lebocins, Drosomycin, Cecropins,Attacins, Defensins, Drosocins, Diptericins, Metchnikowin,and Ponericin; and plenty of them have not yet beenidentified. Insect AMPs are highly potent due to theirinhibitory concentration, which ranges in low molar level.However until now, no insect AMPs have been available inthe market, but there is no doubt soon these insect AMPsmay dominate the existing therapeutic antibiotics.28 Theinsect ladybird Harmonia axyridis is identified to produceabout 50 types of AMPs.Figure 1. The Schematic Structures of the Gram-negative and -Positive Bacteria Cell Membranes and the Mode of Action of Antimicrobial Peptideson the Cell Membrane.23http://www.biotechrep.irJ Appl Biotechnol Rep, Volume 8, Issue 3, 2021 194
Mohideen and LouisTypes of Insect Antimicrobial PeptidesAMPs are divided into three groups: (a) Cecropins, definitepeptides having only α–helices, (b) Defensins having 6-8continuous cysteine amino acids, and (c) peptides with ahigh representation of specific amino acids.(a) CecropinsCecropins are small proteins belonging to the family ofcationic AMPs ranging in length from 35-38 non-cysteineresidues. They were first discovered in the vaccinated hemolymphof Hyalophora cecropia pupae from which the termCecropins was derived. They have also been identified fromother insect families like Lepidoptera, Diptera, and Coleoptera.These are highly active on both gram-positive and gramnegative bacteria and also in some fungi.29 Cecropins frominsects are also called as Sarcotoxin, lepidopteran, andBactericidin. These classes of AMPs will have an N-terminaltryptophan residue and amidated C-terminal.30 The cecropinsare classified into several types based on their structure,namely, (Cecropin-A, Cecropin-B, Cecropin-C, Cecropin-D).All these types have been previously explained in detail.31(b) DefensinsDefensins are the second primary structural class of insectAMPs. Host defense is the vital role of defensins as effectorsand regulators. They are classified into two types, namely αDefensins and β- Defensins. They are cationic peptides witharginine residues having antibiotic activity against vastmicroorganisms.33 They have a predominant β-sheet globularstructure, are stabilized by intramolecular disulfide bridges,and are widely distributed across insect orders. 34 The first ofthe defensins were discovered in the flesh fly Phormiaterranovae containing six cysteine residues. It was found tobe most active against gram-positive bacteria primarily andfew gram-negative bacteria. Defensins from insects areisolated from various insect orders, namely Coleoptera,Hemiptera, Diptera, Trichoptera, Hymenoptera, and Odonata.35A few insect defensins can act against filamentous fungispecies also, e.g., Gallerimycin from Galleria mellonella, agreater wax moth.35–38Table 1. Cecropins Identified from Insects, their Amino Acid Sequences and their Sources 31,32NameAmino Acid SequenceCecropin AGGLKKLGKKLEGVGKRVFKASEKALPVAVGIKALG-NH2Cecropin BKWKVFKKIEKMGRNIRNGIVKAGPAIAVLGEAKAL-NH2Cecropin B1KWKVFKKIEKMGRNIRNGIVKAGPKWKVFKKIEK-NH2Cecropin B3AIAVLGEAKALMGRNIRNGIVKAGPAIAVLGEAKAL-NH2Cecropin in DWNPFKELEKVGQRVRDAVISAGPAVATVAQATALAK-NH2Cecropin GKKIERVGQHTRDATIQTIGVAQQAVNVAATLKGTable 2. Defensins Identified from Insects, their Amino Acid Sequences and their Sources33,36NameAmino Acid GSFANVNCWCETInsect in AATCDLLSGTGINHSACAAHCLLRGNRGGYCNGKAVCVCRNSapecin BLTCEIDRSLCLLHCRLKGYLRAYCSQQKVCRCVQSapecin CATCDLLSGIGVQHSACALHCVFRGNRGGYCTGKGICVCRNTenecin LSGRYKGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGCGalleria GGFRFDichotoma R(c) Peptides with a High Representation of Specific Amino AcidsThis section of the review highlights a more significantnumber of AMPs identified until now. Those peptides witha high content of certain residues, like glycine, tryptophan,arginine, and histidine-rich residues are Attacins, Drosocins,Moricins, Lebocines, Diptericines, Metchnikowin, Ponericins,and Jelleines.17,31AttacinsAttacins rich in glycine residues were first identified in thehemolymph of H. cecropia. It has a molecular mass of about20-23 kDa and isoelectric point 5.7-8.3. It is more effective195 J Appl Biotechnol Rep, Volume 8, Issue 3, 2021SourceAedes albopictusAntheraea pernyiAntheraea pernyiAntheraea pernyiH. CecropiaH. CecropiaAscaris suumLucilia eximiaSourceHeliothis virescensAeschna cyaneaPhormia terranovaeSarcophaga peregrinaSarcophaga peregrinaSarcophaga peregrinaTenebrio molitorPseudacanthotermes spinigerDrosophila melanogasterGalleria mellonellaApis melliferaAllomyrina dichotomaagainst gram-negative bacteria. It is distinguished intoseveral types from A-F and classified into two majorcategories acidic and basic Attacins. They are also reportedfrom various insects, namely Helicoverpa armigera, Glossinamorsitans, Heliothis virescens, Trichoplusia ni, Muscadomestica, and Manduca sexta.39,40Table 3. Attacins Identified from Insects, their Amino Acid Sequencesand their Sources17NameAmino Acid SequenceSourceAttacins A-D AGALTINSDGTSGAVVKVPI Hyalophora cecropiaAttacins E-FDAHGALTLNSDGTSGAVV Hyalophora cecropiaKVPFAGNDLNIhttp://www.biotechrep.ir
Insect Antimicrobial PeptidesMoricinsThese were first identified from B. mori by bacterial injection.They do not have amino acid residue modifications like αamidation of C-termini present in cecropins and the hydroxylationof lysine residues.41 They actually have a high permeability ratioof the bacterial membrane due to the amphipathic N-terminalsegment of α-helix. Moricins have shown positive results ininhibiting the growth of both gram-positive and gram-negativebacteria (gram-positive bacteria to a large extent).42,43Table 4. Moricin and its Amino Acid Sequences with the Source ofIdentification42NameAmino Acid mbyx moriANDVFNFLKPKKRKADrosocinsThese were first identified from Drosophila melanogasterand were conserved in the entire Drosophila genus (19amino acid residues).31 Drosocins have high resistance togram-negative bacteria, and some proline-rich drosocin i.e.,glycosylated drosocin shows potential activity against E.coli.44 They are highly capable against bacteria and fungidue to certain pore-forming peptides, which help in theirentry into the cell membrane.9 Apidaecin produced byhoneybee is a homolog to drosocin.45Table 5. Drosocin and its Amino Acid Sequences with the Source ofIdentification18NameAmino Acid SequenceSourceDrosocin GKPRPYSPRPTSHPRPIRVDrosophila melanogasterLebocinsLebocins were first discovered in B. mori (silkworm) thatwas inoculated with E. coli. They are naturally rich inproline peptide with O-glycosylated 32 residues.41 They arehighly reactive on both gram-positive and gram-negativebacteria and fungi. This AMP has been reported from otherlepidopteran species, namely, Manduca sexta, Trichoplusiani, Pseudoplusia includens, S.cynthia, Pieris rapae, andAntheraea pernyi. Lebocin has 41% sequence homology toApis mellifera produced Abaecin.29,46-49Table 6. Lebocin and its Amino Acid Sequences with the Source ofIdentification41NameAmino Acid SequenceSourceLebocin DLRFLYPRGKLPVPTPPPFNPKPIYIDMGNRY Bombyx moriDiptericinThis family consists of glycine-rich antibacterial peptideweighs about 8kDa with 82 amino acid residues. It has beenidentified from insects of various families, namely Phormiaterranovae, Mayetiola destructor, Sacrophaga peregrina,and also in Drosophila melanogaster. It is more activeagainst specific gram-negative bacteria (Erwinia carotovora,E.coli K12, Erwinia nericola T).35http://www.biotechrep.irTable 7. Diptericin and its Amino Acid Sequences50NameAmino Acid SourceSarcophagaperegrinaJelleinesJelleines are a type of insect antimicrobial peptide isolatedfrom the Royal jelly of Apis mellifera. They consist of 8-9amino acid residues with a charge of 2.51,52 Four types ofAMPs have been identified and isolated from royal jelly,namely Jelleines 1, Jelleines 2, Jelleines 3, and Jelleines 4.These were active against both gram-positive and gramnegative bacteria and also fungi.23Table 8. Jelleines Identified from Apis mellifera and their Amino AcidSequences52NameAmino Acid SequenceSourceJelleines 1PFKLSLHLJelleines 2TPFKLSLHLApis melliferaJelleines 3EPFKLSLHLJelleines 4TPFKLSLHMetchnikowinIt has been named after the Russian scientist ElieMetchinikoff. It is a proline-rich peptide with 26 amino acidresidues identified from D. melanogaster. Metchnikowin isactive against gram-positive bacteria and fungi and showsno activity against gram-negative bacteria. It can bind toribosomes of microbes, which prevents protein translation. 53This peptide also interacts against an important fungal cellwall synthesizing enzyme called β-(1,3) glucanosyl transferaseGel 1. According to the study of Moghaddam et al., it hasinhibited around 52% SDH activity of Fusarium graminearum.54Table 9. Metchnikowin and its Amino Acid Sequences53,54NameAmino Acid sophilaPGPIYmelanogasterPonericinsThey were first identified and isolated from the predatoryant venom of Pachycondyla goeldii, which is from thesubfamily Ponerinae.55 Based on the primary structuresimilarities, they are divided into three families, namelyPonericins G, Ponericins L, and Ponericins W. The cellmembrane of Ponericins have an α-helical structure.56Insect AMPs in the Field of Therapeutics and MedicineDue to various modes of action of AMPs, they are morepotent than conventional antibiotics which makes them anideal candidate for new antibiotics.57,58 AMPs neutralizeendotoxin ability, considerably low Minimum InhibitoryConcentration (MIC) and show that they are highly capableof killing bacteria. They show potential activity againstbiofilms, which also showed resistance to traditionalantibiotics. In addition to that, the potential AMPs haveJ Appl Biotechnol Rep, Volume 8, Issue 3, 2021 196
Mohideen and LouisTable 10. Ponericins Identified from Pachycondyla goeldii and their Amino Acid Sequences31,56NameAmino Acid SequencePonericins W1WLGSALKIGAKLLPSVVGLFKKKKQPonericins W2WLGSALKIGAKLLPSVVGLFQKKKKPonericins W3GIWGTLAKIGIKAVPRVISMLKKKKQPonericins W4GIWGTALKWGVKLLPKLVGMAQTKKQPonericins W5FWGALIKGAAKLIPSVVGLFKKKQPonericins W6FIGTALGIASAIPAIVKLFKPonericins G1GWKDWAKKAGGWLKKKGPGMAKAALKAAMQPonericins G2GWKDWLKKGKEWLKAKGPGIVKAALQAATQPonericins G3GWKDWLNKGKEWLKKKGPGIMKAALKAATQPonericins G4DFKDWMKTAGEWLKKKGPGILKAAMAAATPonericins G5GLKDWVKIAGGWLKKGPGILKAAMAAATQPonericins G6GLVDVLGKVGGLIKKLLPPonericins G7GLVDVLGKVG GLIKKLLPGPonericins L1LLKELWTKMKGAGKAVLGKIPonericins L2LLKELWTKIKGAGKAVLGKIKGLLshown a wide range of anticancer and antiviral properties.There are several hindrances for the activity of AMPs onhumans, like some synthetic degradation pathways, namelyβ-elimination, hydrolysis, oxidation, isomerization, anddeamination.To overcome hindrances, AMPs are now produced inpharmaceutical industries as L and D amino acids, whichhelps them to withstand proteolytic degradation.24 Thecancer cell has a resisting property called MultidrugResistance (MDR), which makes them more drug-resistant.Some AMPs are also capable of killing cancer cells rapidlyand have easier absorption with lower side effects.However, it has a greater disadvantage in the form of toxicity,permeability, stability, and route of drug administration. 59To screen potential AMP libraries, high throughputsequencing is being used, which was first used in theprocess of drug development in the late 1980s. As to theUnited Kingdom's five-year antimicrobial strategy 20132018, the number of highly resistant pathogens are rapidlyincreasing which will become increasingly difficult tomaintain the public and animal health welfare. There is anurgent need for the development of new antibiotics,diagnostic methods, and novel therapies by promotinginnovation and investment in the development of newTable 11. Few Insect-based AMPs with Therapeutic PropertiesS. No Name/Class of AMPSource/OrderG. mellonellaH. cecropia1Cecropin A2Cec B3Cec XJ4Cec XJ5Cec XJ6CSαβ - DLP2 and DLP47DefensinDiptera, Hymenoptera,Coleoptera,Lepidoptera,Hemiptera, Isoptera, Odonata8Tenecin - 1 & 39Hecate (Derivative ofmelittin)Alloferons10SourcePachycondyla goeldiiresistant drugs. The AMPs were identified as alternativesfor antimicrobials.30,32,60 One of the AMP identified fromthe mosquito Aedes aegypti namely (BR003-Cecropin A), iseffective against gram-negative bacteria. Recently, antimicrobialagents were identified using high throughput sequencingapproaches, that are found to target Pseudomonas aeruginosa,Candida albicans.61,62Table 11 gives a hint of few insect AMPs reported to havetherapeutic properties. Some AMPs have shown the effectof immune-stimulation by provoking the process ofchemokines, cell migration, and cell proliferation. Currently,there are more insect derived AMPs which are effectiveagainst pathogens affecting humans, namely, Citrobacterfreundii, Euterobacter aerogenes, K.pneumonia, andLegionella dumoffei.18,36,63-65 Some of the fungal species thatare prone to some types of insect antimicrobial peptidesinclude Pichia pastoris, Trichoderma viridae, andAspergillus fumigatus. Various insect AMPs have beenidentified, including Mellitin derived from honeybee, whichis effective against Herpus simlex virus and two types ofalloferons identified from blowfly that are effective againsttype A and type B Human influenza virus.30,66,67 The needfor developing AMPs as a tool against AMR 68 and theirresistance mechanisms has been also well documented.69ApplicationReferenceDestroys planktonic and sessile biofilm-forming UPEC cells79Improved the survival of mice bearing malignantascites/antitumor activityAntitumor activity proved in mouse models80Inhibits the proliferation of human gastric cancer cells andinduces cell death both in vitro and in vivoInduces cytoskeleton disruption in esophageal carcinoma cells81Antibacterial and immunomodulatory activities of insectdefensins-DLP2 and DLP4 against multidrug-resistant S. aureusEffective against M. luteus, A. viridians, B. megaterium, B.subtilis, B. thuringiensis and S aureus.83T. molitorA. melliferAntineoplastic therapy. Inhibits proliferation of leukaemia cells84Active against Herpes simplex virus 1 (HSV-1)85C. vicinaActive against Human influenza viruses A and B86B. moriB. moriB. moriH. illucens197 J Appl Biotechnol Rep, Volume 8, Issue 3, 2021818284http://www.biotechrep.ir
Insect Antimicrobial PeptidesS. No1Name/Class of AMPAttacin opins A and B7Magainin8Cecropin A9Attacin10Tenecin - 1 & 3Table 12. Few Insect-based AMPs with Agriculture SignificanceSourceApplicationH. cecropiaGets secreted into hemolymph upon bacterialinfection; Phytopathogenic bacteria control of fireblight disease in PearA. meliferaTransgenic potato showed improved activity againstplant pathogenic bacteria belonging to Erwinia andPseudomonas genera. Also active againstSalmonella and Shigella species, Rhizobium andAgrobacterium species andB. cinereaTransgenic tobacco showed resistance to variety ofplant pathogenic bacteriaB. cinereaTransgenic tobacco showed resistance to variety ofplant pathogenic bacteriaS. peregrinaTransgenic tobacco effective againstP.syringae pv. tabaci and E.carotovora ssp. carotovoraB. moriTransgenic rice (Magneporthe grisea, Xanthomonasoryzae) showed significant rersistance to yieldreducing bacterial and fungal speciesMultiple insectsHighly effective against various fungal and bacterialspecies and significantly boosted the resistancewhen expressed in tobaccoG. mellonellaControl of larval Heliothis virescens via microbialentomopathogens and disrupts the immuneresponse against parasitesH. cecropiaResistance to Blackleg and soft rot diseases, causedby the bacterium Erwinia carotovora in potatoT. molitorImportant for the feed industry not only because ofthe protection of animalsInsect AMPs in the Field of AgricultureInsects inflict two types of damage to plants, one physicaland the other that alters its physiological balance. Theproduction losses in the field of agriculture at both pre- andpost-harvest stage is highly immeasurable due to severalmicrobial diseases which reduce the yield of products.About 14% of total loss of all crop production in the entireworld is caused exclusively by microbial diseases. Thebeneficial role of AMPs in agriculture has been welldocumented. Using AMPs in the field of agriculture hasbeen implemented in the 1980s when they were discovered.Still, they showed low activity against certain pathogensand more toxic effects against animal and human cells, sothere is a need for specific AMPs to be designed and used toreduce this cause.72,73 Transgenic expression of plant baseddefensin BrD1 exhibited clear insecticidal potential incomparison to the control. Expression of BrD1 in differentplants may make them resistant to sucking insects.74 Similarfindings have already been reported on wheat, banana andother crops.75 The floral defensins, PhDef1 and PhDef2provide resistance against pathogens of banana.76 Sarcotoxin-IAisolated from flesh fly, when genetically engineered intotobacco plant; dose dependent resistance to Erwinia carotovorasubsp. carotovora (causing wild fire disease), Pseudomonassyringae pv. tabaci, (causing bacterial soft rot disease),Rhizoctonia solani, and Pythium aphanidermatum, wasreported.77,78D. melanogaster based proline-rich AMP Metchnikowin,when expressed in barley showed resistance to differentfusarium spp, species from the phylum Ascomycota and in adose-dependent manner against Basidiomycota 897890,9172929384Fusing the active regions of different AMPs have given riseto chimeric AMPs which improved the impact of theseAMPs on their target pathogens.96,97 Commercially importantspecies of B. mori has been reported to produce six classesof AMPs which renders immunity against the invadingpathogens which include several bacteria 98 Resistance toXanthomonas axonopodis by the transgenic sweet orangehas been attributed to insect based Attacin-A gene codedsignal peptide.99,100 Cecropin boosts significant resistancein tomato plants against two major pathogens of tomatocausing wilt and spot diseases.101 A brief description ofAMPs expressed in transgenic plants that confer partialresistance to pathogens has been well documented 102 and alist of few insect-based AMPs having applications in theagriculture field are listed in Table 12. Another major classof AMPs defensins, such as drosomycin and heliomicinexpressed in tobacco, have proven to be effective against B.cinerea.89 Some of the AMPs from animals have also beenanalyzed for the plant potential such as Magainin from frogand Cercopin from silk moth, mainly used in in-vivo and exvivo studies against the pathogens.71 There are somecomplex factors in the plant micro-environment, whichaffect the activity between the pathogens and AMPs. AMPs,therefore, could well be the future of pest control.Scope and Applications of AMPsDiversity in insects offers an unprecedented scope forexploring human-friendly entities. Various studies, asmentioned earlier, have reported the presence and efficacy ofinsect-based AMPs.104 Further mining of insect genomes andtranscriptomes may well unearth a treasure of biologicallyJ Appl Biotechnol Rep, Volume 8, Issue 3, 2021 198
Mohideen and Louissignificant molecules. There is still a long way to go in thefield of insect AMPs, and these have the potential to replacethe existing drug compounds.Natural therapeutic peptides have some drawbacks, andthese could be overcome by insect AMPs, which couldfurther lead us into peptide mimetics.105 AMPs can play amore significant role in cancer therapeutics, especially skincancer,106 and other infections.105 Their ability to negateresistance mechanisms and their broad-spectrum activitywork in favour of AMPs.107 Homology to mammalian peptideshas been reported, and these could help us understanddifferent human disorders.108 Different AMPs can act asreference molecules that can be fine-tuned; by synthesizingderivatives of these AMP that will have good absorbance,bioavailability, with the least side effects.ConclusionAMPs have been reported from across life-forms and theirpresence in insects is expected to be much higher thananticipated. Insect-based AMPs predicted to thus-far give agreat opportunity to assess their structural, chemical,biological and functional efficacy. Advancements in genomicand proteomic technologies have generated huge data whichcan be analyzed for the prediction of new class of AMPsand their interaction with the respective host’s target. Theclinical usage of AMPs is still limited due to highbioavailability, high specificity, potential hemolysis, lowtoxicity level, and limited drug-drug interaction. Thesuccess achieved in fighting blight and other types ofbacterial and fungal pathogenic diseases through transgenicexpression of attacins, drosocins, cecropins, melittins anddefensins class of AMPs in potato, tomato, pear, tobaccocould be extended to large-scale field-based assessmentsand be extended to other types of crops. Similarly, more invitro and in-vivo studies involving these AMPs could leadus to findi
These peptides will be a stable alternative for antibiotics Abstract Antimicrobial resistance (AMR) has become a menace for humanity. Several antibiotics have become ineffective, and there is a need for a novel route or approach to find solutions. Antimicrobial peptides (AMPs) have already generated a lot of noise for over four decades.
Antimicrobials, Aspergillus fumigatus, Antimicrobial Peptides 1. Introduction 1.1. Antimicrobial Peptides and Proteins It is notable that antimicrobial peptides particularly cationic ones play a signifi-cant role within the natural immunity of animal defences against topical and general microbes altogether species of life. These antimicrobial .
Antimicrobial Peptides 2 ANTIMICROBIAL PEPTIDES OFFERED BY BACHEM Ribosomally synthesized antimicrobial peptides (AMPs) constitute a structurally diverse group of molecules found virtually in all organisms. Most antimicrobial peptides contain less than 100 amino acid residues, have a net positive charge, and are membrane active. They are major
Chapter 5: Antimicrobial stewardship education for clinicians 123 Acronyms and abbreviations 126 5.1 Introduction 127 5.2 Key elements of antimicrobial stewardship education 128 5.2.1 Audiences 128 5.2.2 Principles of education on antimicrobial stewardship 129 5.2.3 Antimicrobial stewardship competencies and standards 129
Virology 15 Mycology 17 Parasitology 17 Interpretation of Viral Diagnostic Tests 19 Antimicrobial Formulary 23 Antimicrobial Costs 25 Antimicrobial Concepts and Tips 27 Antimicrobial Restrictions and . identification and susceptibility testing on most comm
2 The Review on Antimicrobial Resistance, Chaired by Jim O’Neill 3 The Review on Antimicrobial Resistance, Chaired by Jim O’Neill The Review The UK Prime Minister announced a Review on Antimicrobial Resistance in July, call
Several groups in the 1970s and 1980s reported antimicrobial peptides produced from leukocytes, including α-defensins from rabbits and humans [10]. One important landmark in the history of antimicrobial peptides is the work of Boman et al. in 1981. Boman injected bacteria into pupae of a silk moth and isolated the antimicrobial peptides
Plant antimicrobial peptides Plants are constantly exposed to attack from a large range of pathogens. Under attack conditions plants synthesized antimicrobial peptides as innate defence. Thionins were the first antimicrobial peptides to be isolated from plants, and normally consists of 45-48 amino acids.
100 Days of School, 100 Agricultural Activities! 100th Day festivities have been celebrated throughout schools since the school year of 1981-1982. Lynn Taylor introduced the 100th Day of School idea in the Center for Innovation in Education newsletter. Early celebrations focused on developing number sense for young children. Today, preschool children through elementary students celebrate their .
