Bitkisel Antimikrobiyal Peptitler: Yapı, Fonksiyon ve Uygulama Potansiyeli

Öz

Amaç: Antimikrobiyal peptitler (AMP'ler), yaşamın tüm alanlarında doğuştan gelen bağışıklığın bir parçasıdır ve patojenlere karşı güçlü içsel savunma sağlarlar. Bitki AMP'leri, düşük moleküler ağırlıkları, sisteinle stabilize edilmiş yapıları ve termokimyasal kararlılıkları nedeniyle dikkat çekicidir. Bununla birlikte, bitki AMP'lerinin karakterizasyonu mevcut literatürde genellikle yetersizdir. Burada, antimikrobiyal direnç endişelerinin üstesinden gelme potansiyellerini tartışmak ve değerlendirmek için birleşik bir yaklaşımla bitki AMP'lerinin özelliklerini sunmak amaçlanmıştır. Yöntemler: Bu derlemede hem ulusal hem de uluslararası araştırmalar temel alınarak, özellikle tiyoninler, defensinler vb. gibi ana ailelere odaklanılarak, amino asit dizileri, disülfit köprüsüyle stabilize edilmiş üçüncül yapıları, termokimyasal kararlılıkları, hedef spektrumları ve moleküler mekanizmaları sunularak bitki AMP'lerinin karşılaştırmalı bir tartışması yapılmıştır. Sonuçlar: Literatür, bitki AMP'lerinin bakteri, mantar, virüs ve parazitlere karşı geniş spektrumlu antimikrobiyal aktiviteye sahip olduğunu göstermektedir. Disülfit köprüleme kararlılıkları, onları çevresel stres koşullarına karşı dirençli hale getirir. Farklı AMP'lerin, membran degradasyonu, hücre içi süreç değişiklikleri ve büyüme inhibisyonu gibi klasik antibiyotiklere kıyasla farklı etki mekanizmaları vardır. Bu nedenle, direnç oluşturulması zor olan yeni antimikrobiyal ajanlar olarak kabul edilirler. Sonuç: Bu çalışma, bitki AMP'lerinin bitki içsel savunmalarındaki merkezi rolünü kapsamlı bir şekilde sunmakta ve bunların tarımsal araştırmalarda biyopestisitler ve transgenik bitki geliştirme alanlarında ve tıbbi araştırmalarda yeni antimikrobiyal ajanlar olarak kullanım olasılığını vurgulamaktadır. Bununla birlikte, klinik ve endüstriyel uygulamalarda güvenli bir şekilde kullanılabilmeleri için toksisite, kararlılık ve üretim verimliliği ile ilgili kesin özelliklerini ortaya çıkarmak için daha fazla in vivo çalışmaya ihtiyaç vardır.

Etik Beyan

Bu çalışma, insan katılımcılar veya deney hayvanları üzerinde herhangi bir araştırma içermemektedir. Çalışma kapsamında etik kurul izni alınmasını gerektiren bir uygulama bulunmamaktadır. Tüm veriler, daha önce yayımlanmış bilimsel çalışmaların incelenmesine dayalı olarak elde edilmiş olup, bilimsel ve etik ilkelere uygun şekilde gerçekleştirilmiştir. Yazar(lar), araştırma ve yayın etiğine uygun davrandıklarını beyan eder.

Teşekkür

Bu çalışmayı yönlendiren değerli hocama ve katkıda bulunan tüm profesörlere minnettar olduğumu belirtmek isterim. Ayrıca, sarsılmaz maddi ve manevi destekleri için aileme de teşekkür ederim.

Plant Antimicrobial Peptides: Structure, Function, and Application Potential

Öz

Purpose: Antimicrobial peptides (AMPs) are parts of innate immunity in all domains of life, and they provide potent intrinsic defense against pathogens. Plant AMPs are noteworthy due to their low molecular weigths, cystein-stabilized structures, and thermochemical stabilities. However, characterization of plant AMPs is generally loose in the current literature. It was aimed here to present properties of plant AMPs with an unified approach to discuss and evaluate their prospective potential for to overcome antimicrobial resistance concerns. 

Methods: Using both national and international research as basis in this review, comperative discussion of plant AMPs with a particular focus on major families like thionines, defensins etc. was carried out by presenting their amino acid sequences, disulphite bridged stabilized tertiary structures, thermochemical stabilities, target spectrums, and molecular mechanisms. 

Results: Literature is presenting that plant AMPs have wide-spectrum antimicrobial activity against bacteria, fungi, viruses, and parasites. Their disulphite bridged stabilities make them resistant to environmental stress conditions. Different AMPs have different mechanisms of action compared to classical antibiotics such as membrane degregadation, intracellular process alterations, and growth inhibitions. Hence, they are considered as novel antimicrobial agents that are difficult to mount resistance against. 

Conclusion: This study extensively presents the central role of plant AMPs in plant intrinsic defenses, and stresses the possibility of their uses in agricultural research as biopesticides and transgenic plant developments, and in medicinal research as novel antimicrobial agents. However, further in vivo studies are necessary to reveal their precise properties regarding the toxicity, stability, production efficiency to safely use them in clinical and industrial practices.

Anahtar Kelimeler

• Antimicrobial peptides
• Plant defense
• Antimicrobial resistance

Etik Beyan

This study does not involve any research conducted on human participants or experimental animals. Therefore, no ethical committee approval was required for this study. All data were obtained through the review of previously published scientific studies and were conducted in accordance with scientific and ethical principles. The author(s) declare that they have adhered to the principles of research and publication ethics.

Teşekkür

I would like to express my gratitude to my esteemed professor who guided this study and to all the professors who contributed. I would also like to thank my family for their unwavering material and moral support.

Kaynakça

1. 1. Brown KL, Hancock RE. Cationic host defense (antimicrobial) peptides. Curr Opin Immunol. 2006;18(1):24-30.
2. 2. Hancock REW, Sahl HG. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol. 2006;24(12):1551-7.
3. 3. Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol. 2005;3(3):238-50.
4. 4. Lopez-Silva TL, Leach DG, Azares A, Li IC, Woodside DG, Hartgerink JD. Chemical functionality of multidomain peptide hydrogels governs early host immune response. Biomaterials. 2020;231:119667.
5. 5. Zhao X, Wu H, Lu H, Li G, Huang Q. Lamp: A database linking antimicrobial peptides. PLoS One. 2013;8(6):e66557.
6. 6. Conlon JM, Sonnevend A. Antimicrobial peptides in frog skin secretions. Methods Mol Biol. 2010;618:3-14.
7. 7. Radek K, Gallo R. Antimicrobial peptides: Natural effectors of the innate immune system. Semin Immunopathol. 2007;29(1):27-43.
8. 8. Peters BM, Shirtliff ME, Jabra-Rizk MA. Antimicrobial peptides: Primeval molecules or future drugs? PLoS Pathog. 2010;6(10):e1001067.

9. 9. Leippe M. Antimicrobial and cytolytic polypeptides of amoeboid protozoa—Effector molecules of primitive phagocytes. Dev Comp Immunol. 1999;23(4-5):267-79.
10. 10. Campos ML, de Souza CM, de Oliveira KB, Dias SC, Franco OL. The role of antimicrobial peptides in plant immunity. J Exp Bot. 2018;69(21):4997-5011.
11. 11. Tam J, Wang S, Wong K, Tan W. Antimicrobial Peptides from Plants. Pharmaceuticals. 2015;8(4):711-57.
12. 12. Pelegrini P, del Sarto RP, Silva ON, Franco OL, Grossi-de-Sa MF. Antibacterial peptides from plants: What they are and how they probably work. Biochem Res Int. 2011;2011:1-9.
13. 13. Li J, Hu S, Jian W, Xie C, Yang X. Plant antimicrobial peptides: structures, functions, and applications. Bot Stud. 2021;62(1):15.
14. 14. Hammami R, Ben Hamida J, Vergoten G, Fliss I. Plant antimicrobial peptides: classification, mechanisms of action and applications. Appl Microbiol Biotechnol. 2012;93(3):1241-53.
15. 15. Hughes P, Dennis E, Whitecross M, Llewellyn D, Gage P. The cytotoxic plant protein, β purothionin, forms ion channels in lipid membranes. J Biol Chem. 2000;275(2):823-7.
16. 16. Stec B. Plant thionins–the structural perspective. Cell Mol Life Sci. 2006;63(12):1370-85. 17. Silverstein R, Kock KHS, Araya D, Vrijsen M, Thevissen K. The thionin family of antimicrobial peptides. PLoS One. 2021;16(7):e0254549.
17. 18. Steck G, Schäfer W. Plant thionins: structure, biological functions and potential use in biotechnology. Mol Plant Pathol. 2007;8(6):629-40.
18. 19. Gholizadeh A, Ghadamyari M, Khosravani S. Research progress of plant antimicrobial peptides. TMR Integr Med. 2022;6(1):1-8.
19. 20. Graham MA, Silverstein KAT, VandenBosch KA. Defensin-like genes: genomic perspectives on a diverse superfamily in plants. Crop Sci. 2008;48(S1):S3-S11.
20. 21. Stotz HU, Thomson JG, Wang Y. Plant defensins: defense, development and application. Plant Signal Behav. 2009;4(11):1010-12.
21. 22. García-Olmedo F, Molina A, Alamillo JM, Rodríguez-Palenzuéla P. Plant defense peptides. Biopolymers. 1998;47(6):479-91.
22. 23. Carvalho AO, Gomes VM. Plant defensins and defensin-like peptides—biological activities and biotechnological applications. Curr Pharm Des. 2011;17(38):4270-93.
23. 24. van der Weerden NL, Anderson MA. Antifungal plant defensins: mechanisms of action and production. FEMS Microbiol Lett. 2014;353(1):1-9.
24. 25. Segura A, Moreno M, Madueño F, Molina A, García-Olmedo F. Snakin-1, a peptide from potato that is active against plant pathogens. Mol Plant Microbe Interact. 1999;12(1):16-23.
25. 26. Berrocal-Lobo M, Segura A, Moreno M, López G, García-Olmedo F, Molina A. Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. Plant Physiol. 2002;128(3):951-61.
26. 27. Nahirñak V, Almasia NI, Hopp HE, Vignoni E, Carrari F. Snakin/GASA proteins: involvement in hormone crosstalk and redox homeostasis. Plant Signal Behav. 2012;7(8):1004-8.
27. 28. Segura A, Moreno M, García-Olmedo F. Snakin-1, a peptide from potato that is active against plant pathogens. FEBS Lett. 1999;461(2):182-6.
28. 29. Archer BL. The proteins of Hevea brasiliensis Latex. Isolation and characterization of crystalline hevein. Biochem J. 1960;75(2):236-40.
29. 30. Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ. Hevein an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta. 1991;183(2):258-64.
30. 31. Beintema JJ. Structural features of plant chitinases and chitin-binding proteins. FEBS Lett. 1994;350(2-3):159-63.
31. 32. Broekaert WF, Mariën W, Terras FR, De Bolle MF, Proost P, Van Damme J, et al. Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry. 1992;31(17):4308-14.
32. 33. Yeats TH, Rose JK. The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs). Protein Sci. 2008;17(2):191-8.
33. 34. Craik DJ, Daly NL, Bond T, Waine C. Plant cyclotides: A unique family of cyclic and knotted proteins that define the cyclic cystine knot structural motif. J Mol Biol. 1999;294(5):1327-36.
34. 35. Poth AG, Colgrave ML, Lyons RE, Daly NL, Craik DJ. Discovery of an unusual biosynthetic origin for circular proteins in legumes. Proc Natl Acad Sci U S A. 2011;108(25):10127-32.
35. 36. Nguyen GK, Zhang S, Nguyen NT, Nguyen PQ, Chiu MS, Hardjojo A, et al. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family. J Biol Chem. 2011;286(27):24275-87.
36. 37. Nguyen GK, Lian Y, Pang EW, Nguyen PQ, Tran TD, Tam JP. Discovery of linear cyclotides in monocot plant Panicum laxum of the Poaceae family provides new insights into evolution and distribution of cyclotides in plants. J Biol Chem. 2013;288(5):3370-80.
37. 38. Craik DJ, Daly NL, Mulvenna J, Plan MR, Trabi M. Discovery, structure and biological activities of cyclotides. Curr Protein Pept Sci. 2004;5(5):297-315.
38. 39. Göransson U, Sjögren M, Svangård E, Claeson P, Bohlin L. Reversible antifouling effect of the cyclotide cycloviolacin O2 against mussels. J Nat Prod. 2004;67(8):1287-90. 40. Gustafson KR, McKee TC, Bokesch HR. Anti-HIV cyclotides. Curr Protein Pept Sci. 2004;5(5):331-40.
39. 41. Gran L. An oxytocic substance found in Oldenlandia affinis DC. The native, Congo medicine kalata-kalata used to accelerate childbirth. Medd Nor Farm Selsk. 1970;32(12):173-80.
40. 42. Gerlach SL, Mondal D. The abundant biological activities of cyclotides. Chronicles Young Sci. 2012;3(3):169-77.
41. 43. Li J, Hu S, Jian W, Xie C, Yang X. Plant antimicrobial peptides: structures, functions, and applications. Bot Stud. 2021;62(1):15.
42. 44. de Oliveira SSS, Cherene MB, Taveira GB, de Oliveira Mello É, de Oliveira Carvalho A, Gomes VM. Plant Antimicrobial Peptides and Their Main Families and Roles: A Review of the Literature. Curr Issues Mol Biol. 2024;47(1):1.