Role of antimicrobial peptides in plant disease management
•
4 likes•852 views
It is one of the advanced topics in plant disease management, detailed information about antimicrobial peptides and their role in plant disease management is furnished clearly.
Recommended
Recommended
More Related Content
What's hot
What's hot (20)
Similar to Role of antimicrobial peptides in plant disease management
Similar to Role of antimicrobial peptides in plant disease management (20)
More from N.H. Shankar Reddy
More from N.H. Shankar Reddy (20)
Recently uploaded
Recently uploaded (20)
Role of antimicrobial peptides in plant disease management
- 1. welcome
- 2. Role of Antimicrobial peptides in plant disease management A. Vanitha II- M.Sc (Agriculture) Dept.of Plant Pathology Annamalai University
- 3. ❖Introduction ❖History of Anti microbial peptides ❖Structure of Anti microbial peptides ❖Sources of Anti microbial peptides ❖Classification of Anti microbial peptides ❖Mode of action ❖Antimicrobial peptides in the plant defense mechanism ❖Resistance of AMP ❖Conclusion outline
- 4. ANTI MICROBIAL PEPTIDES Part of natural immunity in plants First line of defense against phytopathogens. Short sequence of amino acids Positively charged and are diverse group of plant proteins
- 5. Ampipathicity of the structure makes them interact with the membrane of pathogen and affects its permeability.
- 6. OTHER NAMES Alpha helical antimicrobial peptides Cationic host defense peptide Cationic Antimicrobial peptides Cationic amphipathic peptides Host defense peptides
- 7. History of antimicrobial peptides 1940- Hotchkiss and Dubos named this extract as Gramicidin Named Purothionin and found effective against fungi and bacteria 1970- First plant orginated AMP was isolated by Okada and Yoshizumi from wheat and barley 1939-Dubos extract an antimicrobial agent from soil Bacillus against pneumococci.
- 8. Source of ANTI MICROBIAL PEPTIDES Bacteria Fungi Algae Insect Mammals
- 9. ORIGIN SOURCE AMP Animal Cow Lactoferrin Frog skin Esculentin-1 Insect Moth haemolymph Cecropin A,B Fruit fly Sarcotoxin IA Plant Barley Hordothionin Radish Rs-AFP2 Bacteria Pseudomonas Pseudophomins Pantoea pantocins Human Epithelia Bombinin
- 10. STRUCTURE OF ANTIMICROBIAL PEPTIDES Alpha helix Beta sheet Extended Loop
- 11. Classification of antimicrobial peptides 1)Based on their source Non disulfide bridged peptides Peptides with disulfide group 2)Based on their nature Synthetic non ribosomal peptides Synthetic ribosomal/ Natural peptides
- 12. 4)Based on their target microorganism Antifungal Antibacterial Antiparasitic Antiviral 3)Based on their electrostatic charge Cationic peptides Non cationic peptides
- 13. INTERACTION MODEL OF amp BARREL STAVE MODEL TOROIDAL PORE WORM HOLE
- 14. DETERGENT LIKE PEPTIDE CARPET MODEL
- 15. Mode of action Interaction with membrane Transfer acyl monomer Affect biological activity Inhibition of cell wall synthesis Bursting of hyphal tip Binding with phospholipids Altering cell signals
- 17. thionins Balls et al. (1942) identified thionins for the first time in cereals and classified as plant toxins due to their toxic effect towards microbes. They consist of 45-48 amino acids with mainly conserved residues
- 18. BASED ON THEIR CYSTEINE RESIDUE Six cysteine residue Three disulfide bridges Eight cysteine residue Four disulfide bridges Crambin Viscotoxins Phoratoxins α/β- purothionins α/β- hordothionins Hellethionin-D
- 19. STRUCTURAL MODEL OF THIONIN AND PHOSPHOLIPIDS INTERACTION (Stec et al., 2000) Interaction between thionin and phospholipids Dimer stabilization by Asn 11 & Asn14 Bind inorganic phosphate Monomer formation Phospholipids segregation Ion leakage and lysis
- 20. Hydrophobic nature Cationic (except crambin) FEATURES OF THIONIN Both antifungal and antibacterial Except both α and β-purothionins
- 21. Thionins Source Target pathogen References Thionin 2.4 Wheat Fusarium graminearum Asano et al. (2013) Asthi1 Oats Burkholderia plantarii B. glumae Iwai et al. (2002) α/β- Purothionin wheat Pseudomonas solanacearum, Xanthomonas campestris, X.phaseoli, Corynebacterium spp. De Caleya et al. (1972) Examples
- 22. Supportive article Tomoyo Asano et al.(2013)
- 23. Tomoyo Asano et al.(2013)
- 24. Tomoyo Asano et al.(2013)
- 25. DEFENSINS ▪ In 1990, Mendez et al. isolated defensins from barley and wheat and named as Defensins (Gamma thionin). ▪ In 1995, Terras et al. used the termed plant defensin. ▪ Expression of plant defensins are also induced by abiotic stress (drought, saline, temperature) and signaling molecules like ethylene, salicylic acid, methyl jasmonate.
- 26. Based on their effect on pathogenic fungi Morphogenic plant defensins Non- morphogenic plant defensins Inhibit the growth and branching of hyphae Inhibit only hyphal growth But not cause signifigcant morphological damage
- 27. Mode of action of defensins
- 28. Defensins Source Target pathogen Reference SPD1 Ipomoea batatus Fungal and bacterial pathogens Craik et al. (2006) AFP Aspergilus giganteus Botrytis cinerea, Fusarium, Pyricularia oryzae Vila et al. (2001) Examples
- 29. Supportive article Vila et al.(2001)
- 31. LIPID TRANSFER PROTEINS (LTP) ❖ Small cysteine-rich peptides having molecular masses of lower than 10KDa. ❖ It consists of 70-100 amino acid with low molecular weight of 7-10 Kda. ❖ They are cationic peptides with a conserved pattern of four to five-disulfide bridges having eight or ten cys-cys bonds which make structure of the LTPs more stable and heat resistant
- 32. ❖ Expression of lipid transfer proteins can be induced by abiotic stress like saline, drought, NaCl, cold and ABA. ❖ LTPs having synergistic activity with thionins against Clavibacter ssp. Crop LTP Induced by Rice OsLTPd11 Drought Maize 14 LTP Saline,Drought Wheat TaLTP 1.2 & 1.13 Chilling, Wounding
- 33. Lipid transfer proteins Source Target pathogen Reference Ca-LTP Capsicum annum Candida albicans, saccharomyce s cerevisiae Cruz et al. (2010) Ps-LTP1-3 Pisum sativum Fusarium solani, Fusarium oxysporum Bogdanov et al.(2016) Gt-LTP2 Gentiana triflora Botrytis cinerea Akinori kiba et al.(2011) Example:
- 34. Supportive article Kiba et al.(2011)
- 36. Hevein-like plant antimicrobial protiens Archer isolated hevein like plant AMP from rubber tree (Hevea brasiliensis) latex. Heveins are small antimicrobial proteins of 42-45 amino acids and of 4.7KDa with conserved residues of glycine and aromatic acids. They are cationic proteins having 3-5 disulfide bonds.
- 37. Based on the number of cysteine residues Three disulfide bridge Six cysteine residue 6C-hevein Four disulfide bridge Eight cysteine residue 8C-hevein Five disulfide bridge Ten cysteine residue 10C-hevein
- 38. Hevein Source Against pathogen Reference M -hevein Mulberry Trichoderma viride Zhao et al.(2011) GAFP G.biloba Fusarium graminearum , A.alternata Huang et al.(2000) Example
- 39. Supportive article Huang et al.(2000)
- 41. KNOTTIN-TYPE PROTEINS ➢ Nguyen et al.(1990) isolated it from Mirabilis jalapa. ➢ Have cystein knotted triple stranded β-sheet. ➢ Based on the structure they termed as knottin for this molecular scaffold.
- 43. WIDE RANGE OF BIO-ACTIVITIES Enzyme inhibitory action Cytotoxic effect Antimicrobial activity Insecticide Anti-HIV activity α-amylase inhibition Trypsine inhibitors
- 44. Knottins Source Against pathogen Reference Cy-AMP1 Cycas revoluta Fungi and bacteria Yokohama et al.(2009) Wr-A11 Wr-A12 Wrightia religiosa Tenebrio molitor Nguyen et al. (2014) Examples
- 45. Supportive article Yokoyama et al.(2009)
- 47. cyclotides • Cyclotides are naturally occurring cyclic proteins of about 28-37 aminoacids. • Their head-to-tail cyclic peptide back-bone and a knotted arrangement of three disulfide bonds is a unique structural feature of these plant proteins.
- 48. cyclotides • They are found abundantly in Violaceae, Rubiaceae and Cucurbitaceae
- 49. Based on the presence and absence of cis-proline in loop 5 of the peptide backbone Mobius family Twist in backbone Proline –Aminoacid in loop 5 followed by bond in cys 5 and 6 Bracelet family Lack proline residue in loop short helical segment in between third and fourth cys residue of loop3 Trypsin inhibitors Differ from the primary structure from Mobius & Bracelet cyclotide But retain the conserved cystine knot motif
- 50. Hemolytic activity response for insecticidal properties Kalata B1 interrupt epithelial cell in midgut of lepidopteran larvae Interact directly with phosphatidylethanolamine phospholipids of the membrane Leads to vesicle formation Bending of membrane
- 51. Cyclotides Source Against pathogen Reference Kalata B2 Oldenlandia affinis Helicoverpa armigera Craik et al. (2006) Kalata B8 Oldenlandia affinis Antiviral Daly et al. (2006) EXAMPLES:
- 52. Supportive article Craik et al.(2005)
- 55. bacteriocins ▪ Ribosomal synthesized antimicrobial peptides ▪ Produced by bacteria ▪ Kill or inhibit closely related bacterial strains
- 56. Bacteriocins Source Against pathogen Galtrol Agrobacterium radiobacter 48 Agrobacterium tumefaciens Nogall Agrobacterium radiobacter K1026 Agrobacterium tumefaciens Histick N/T Bacillus subtilus St MB1600 Fusarium, Rhizoctonia, Aspergillus Examples
- 57. peptaibols ❑ Linear peptides, usually composed of a C- terminal amino alcohol and an acyl N-terminus. ❑ Non ribosomal synthesized antimicrobial peptides ❑ Affect fungi and plant pathogenic gram positive bacteria
- 58. Peptaibols Source Against pathogen Reference Trichokonins Trichoderma koningii Clavibacter migiganesis, Fusarium oxysporum , Botrytis, Bipolaris Xiao-yan et al. (2006) Harzianins and Trichorzins Trichoderma harzianum Sclerotium cepivorum Goulard et al. (1995) Examples:
- 59. cyclopeptides ❖ D and L- form as well as allo- and diamino derivatives, arranged in a cyclic ring, usually without disulphide bridges. ❖ Lipid cyclopeptides are produced by several plant associated and soil inhabiting bacteria .
- 60. Examples: Cyclopeptides Source Against pathogen Reference Pseudophomins Pseudomonas fluorescens Leptosphaeria maculans, Sclerotinia sclerotiorum. Pedras et al. (2003) Massetolide Pseudomonas fluorescens Pythium intermedium De souza et al. (2003) Iturin Bacillus subtilus Monilinia fructicola Gueldner et al.(1988)
- 61. pseudopeptides ➢ Amide of an amino acid that does not occur in natural peptides ➢ Have few peptide bonds and complex amino acid modification ➢ Produced by bacteria.
- 62. Pseudo peptides Source Against pathogens Reference Blasticidins Bacillus cereus K55-S1 Pyricularia oryzae Copping et al. (2000) Mildiomycin Streptoverticillium rimofaciens B-98891 Podoshera, Sphaerotheca Eryshipe, Uncinula Copping et al. (2000) Pantocines Pantoea agglomerans Erwinia amylovora Brady et al. (2003) Examples:
- 63. SYNTHETIC AMP
- 64. Synthetic AMP can produced by three methods CULTURE OF INDUSTRIAL MICROORGANISM GENETICALLY MODIFIED MICROORGANISM ENZYMATIC HYDROLYSIS OF PROTEINS
- 66. COMMERCIAL PRODUCTS OF AMP NOGALL SUBTILE
- 68. Multiple genes transformation Genetic transformatiom : one target gene is transformed in plant Gene stacking – more than one gene is needed to be transformed for imporved, durable and highly effective resistance against phytopathogen. Cry1AC and Cry2Ab2 genes were transformed in Bt cotton and the transgenic plants were found very effective against pink bollworm.
- 69. conclusion Genetic engineering and genome targeting tools have made it possible to over express the AMPs in the target plant species for imparting enhanced disease resistance. AMP is an alternative to conventional antibiotics