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Antimicrobial Peptides with Plant Origin

Received: 14 March 2016    Accepted: 16 March 2016    Published: 8 December 2016
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Abstract

According to the World Health Organization plants are one of the best sources to obtain a huge variety of biologically active compounds. Human population during centuries has used plants and plants extracts in ethno medicine to cure wide range of diseases. In the scope of modern methods of isolation and purification of different plant substances, antimicrobial peptides (AMPs) give us the opportunity to have a new ally in the fight with different microbial pathogens. Possible future uses of AMPs derived from plants could be either as a new class of anti-infective medications or as bio-preservatives in foods and beverages.

Published in International Journal of Nutrition and Food Sciences (Volume 5, Issue 6-1)

This article belongs to the Special Issue Analytical and Microbiological Characterization of Antimicrobial Peptides

DOI 10.11648/j.ijnfs.s.2016050601.12
Page(s) 5-9
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Plant AMPs, Antimicrobial Action, AMPs Properties

References
[1] B. P. H. J. Thomma, B. P. A. Cammue, K. Thevissen. Plant Defensins. Planta. Vol. 216, No. 2, 2002, pp. 193-202.
[2] F. T. Lay, M. A. Anderson. Defensins-Components of the Innate Immune System in Plants. Current Protein & Peptide Science. Vol. 6, No. 1, 2005, pp. 85-101.
[3] H. Loeza-Ángeles, E. Sagrero-Cisneros, L. Lara-Zárate, E. Villagómez-Gómez, J. E. López-Meza, A. Ochoa-Zarzosa. Thionin Thi2.1 from Arabidopsis thaliana Expressed in Endothelial Cells Shows Antibacterial, Antifungal and Cytotoxic Activity. Biotechnology Letters. Vol. 30, 2008, pp. 1713-1719.
[4] P. Barbosa Pelegrini, R. P. del Sarto, O. N. Silva, O. L. Franco, and M. F. Grossi-De-Sa. Antibacterial Peptides from Plants: What They Are and How They Probably Work. Biochemistry Research International. Vol. 2011, 2011, 250349.
[5] H. U. Stotz, F. Waller, K. Wang. Innate Immunity in Plants: the Role of Antimicrobial Peptides. In Antimicrobial Peptides and Innate Immunity. P. S. Hiemstra, S. A. J. Zaat, Eds. Broken Arrow: Springer Science&Business Media, 2013, pp. 29-51.
[6] A. A. Bahar, D. Ren. Antimicrobial Peptides. Pharmaceuticals. Vol. 6, No. 12, 2013, pp. 1543-1575.
[7] G. Wang, ed. Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies. CABI, England, 2010.
[8] G. Wang. Improved methods for classification, prediction, and design of antimicrobial peptides. Methods in Molecular Biology. Vol. 1268, 2015, pp. 43-66.
[9] L. P. Vernon, G. E. Evett, R. D. Zeikus, W. R. Gray. A Toxic Thionin from Pyrularia pubera: Purification, Properties, and Amino Acid Sequence. Archives of Biochemistry & Biophysics. Vol. 238, No. 1, 1985, pp. 18-29.
[10] M. Berrocal-Lobo, A. Molina, P. Rodríguez-Palenzuela, F. García-Olmedo, L. Rivas. Leishmania donovani: Thionins, Plant Antimicrobial Peptides with Leishmanicidal Activity. Experimental Parasitology. Vol. 122, 2009, pp. 247-249. doi:10.1016/j.exppara.2009.03.019
[11] J. Evans, Y. D. Wang, K. P. Shaw, L. P. Vernon. Cellular Responses to Pyrularia Thionin are Mediated by Ca2+ Influx and Phospholipase a2 Activation and Are Inhibited by Thionin Tyrosine Iodination. PNAS. Vol. 86, 1989, pp. 5849-5853.
[12] P. Desjeux. Leishmaniasis: Current Situation and New Perspectives. Comparative Immunology, Microbiology & Infectious Diseases. Vol. 27, 2004, pp. 305-318. doi: 10.1016/j.cimid.2004.03.004.PMID15225981.
[13] K. Apel, I. Andresen, W. Becker, K. Schluter, J. Burges, B. Parthier. The Identification of Leaf Thionin as One of the Main Jasmonate-Induced Proteins of Barley (Hordeum vulgare). Plant Molecular Biololgy. Vol. 19, No. 2, 1992, pp. 193-204.
[14] D. E. Florack, W. J. Stiekema. Thionins: Properties, Possible Biological Roles and Mechanisms of Action. Plant Molecular Biololgy. Vol. 26, No. 1, 1994, pp. 25-37.
[15] M. Bruix, M. A. Jimenez, J. Santoro, C. Gonzalez, F. J. Colilla, E. Mendez, M. Rico. Solution Structure of Gamma 1-H and Gamma 1-P Thionins from Barley and Wheat Endosperm Determined by 1H-NMR: a Structural Motif Common to Toxic Arthropod Proteins. Biochemistry. Vol. 32, No. 2, 1993, pp. 715-724.
[16] R. W. Osborn, S. Torrekens, J. Vanderleyden, W. F. Broekaert, B. P. Cammue, F. R. Terras, F. Van Leuven. A New Family of Basic Cysteine-Rich Plant Antifungal Proteins from Brassicaceae species. FEBS Letters. Vol. 316, No. 3, 1993, pp. 233-240.
[17] M. Richardson, C. Bloch Jr. A New Family of Small (5 kDa) Protein Inhibitors of Insect Alpha-Amylases from Seeds of Sorghum (Sorghum bicolar (L) Moench) Have Sequence Homologies with Wheat Gamma-Purothionins. FEBS Lett., Vol. 279, No. 1, 1991, pp. 101-104.
[18] N. Ishibashi, D. Yamauchi, T. Minamikawa. Stored mRNA in Cotyledons of Vigna unguiculata Seeds: Nucleotide Sequence of Cloned cDNA for a Stored mRNA and Induction of its Synthesis by Precocious Germination. Plant Molecular Biology. Vol. 15, No. 1, 1990, pp. 59-64.
[19] Y. Choi, Y. D. Choi, J. S. Lee. Nucleotide Sequence of a cDNA Encoding a Low Molecular Weight Sulfur-Rich Protein in Soybean Seeds. Plant Physiology. Vol. 101, No. 2, 1993, pp. 699-700.
[20] L. Padovan, M. Scocchi, A. Tossi. Structural Aspects of Plant Antimicrobial Peptides. Current Protein & Peptide Science. Vol. 11, 2010, pp. 210-219.
[21] P. B. Pelegrini, O. L. Franco. Plant Gamma-Thionins: Novel Insights on the Mechanism of Action of a Multi-Functional Class of Defense Proteins. International Journal of Biochemistry & Cell Biology. Vol. 37, 2005, pp. 2239-2253.
[22] F. Fant, W. Vranken, W. Broekaert, F. Borremans. Determination of the Three-Dimensional Solution Structure of Raphanus sativus Antifungal Protein 1 by 1h nmr. Journal of Molecular Biology. Vol. 279, 1998, pp. 257-270.
[23] M. Fujimura, Y. Minami, K. Watanabe, K. Tadera. Purification, Characterization, and Sequencing of a Novel Type of Antimicrobial Peptides, fa-amp1 and fa-amp2, from Seeds of BuckWheat (Fagopyrum esculentum Moench.). Bioscience, Biotechnology & Biochemistry. Vol. 67, 2003, pp. 1636-1642.
[24] N. Sitaram. Antimicrobial Peptides with Unusual Amino Acid Compositions and Unusual Structures. Current Medicinal Chemistry. Vol. 13, 2006, pp. 679-696.
[25] J. P. Tam, S. Wang, K. H. Wong, W. L. Tan. Antimicrobial Peptides from Plants. Pharmaceuticals. Vol. 8, 2015, pp. 711-757. doi:10.3390/ph8040711
[26] J. J. Beintema. Structural Features of Plant Chitinases and Chitin-Binding Proteins. FEBS Letters. Vol. 350, 1994, pp. 159-163.
[27] J. C. Kader. Lipid-Transfer Proteins in Plants. Annual Review of Plant Physiology and Plant Molecular Biology. Vol. 47, 1996, pp. 627-654.
[28] T. Ke, H. Cao, J. Huang, F. Hu, J. Huang, C. Dong, X. Ma, J. Yu, H. Mao, X. Wang, Q. Niu, F. Hui, S. Liu. EST-Based in Silico Identification and in vitro Test of Antimicrobial Peptides in Brassica napus. BMC Genomics. Vol. 16, 2015, p. 653. doi:10.1186/s12864-015-1849-x
[29] H. Cao, T. Ke, R. Liu, J. Yu, C. Dong, M. Cheng, J. Huang, S. Liu. Identification of a Novel Proline-Rich Antimicrobial Peptide from Brassica napus. mBio. Vol. 6, 2015, e01251-15. doi:10.1128/mBio.01251-15
[30] T. L. Jiang, H. Y. Wu, G. H. Shen, X. H. Dong, Z. Q. Zhang. Antibacterial Activity and Stability of Antimicrobial Peptides in Chinese Prickly Ash Seed Proteins. Modern Food Science & Technology. Vol. 31, 2015, pp. 129-135.
[31] S. Fedhila, W. B. Lazhar, T. Jeridi, V. Sanchis, M. Gohar, D. Lereclus, J. B. Hamida. Peptides Extracted from Artemisia alba Herba Have Antimicrobial Activity Against Foodborne Pathogenic Gram-Positive Bacteria. African Journal of Tradicional, Complimentary and Alternative Medicine. Vol. 12, 2015, pp. 68-75.
[32] A. A. Astafieva, E. A. Rogozhin, T. I. Odintsova, N. V. Khadeeva, E. V. Grishin, Ts. A. Egorov. Discovery of Novel Antimicrobial Peptides with Unusual Cysteine Motifs in Dandelion Taraxacum officinale Wigg. Flowers. Peptides. Vol. 36, 2012, pp. 266-71. doi: 10.1016/j.peptides.2012.05.009
[33] A. Segura, M. Moreno, F. Madueno, A. Molina, F. Garcia-Olmedo. Snakin-1, a Peptide from Potato that Is Active Against Plant Pathogens. Molecular Plant-Microbe Interactions Journal. Vol. 12, No. 1, 1999, pp. 16-23.
[34] M. Berrocal-Lobo, A. Segura, M. Moreno, G. Lopez, F. Garcia-Olmedo, A. Molina. Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. Plant Physiology. Vol. 128, 2002, 951-961.
[35] The Antimicrobial Peptides Database, Departement of Pathology and Microbiology, UNMC, 2016, http://aps.unmc.edu/ AP/main.php.
Cite This Article
  • APA Style

    Zdraveva Petranka, Yotova Maya, Kaloyanov Kaloyan, Pencheva Ivanka. (2016). Antimicrobial Peptides with Plant Origin. International Journal of Nutrition and Food Sciences, 5(6-1), 5-9. https://doi.org/10.11648/j.ijnfs.s.2016050601.12

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    ACS Style

    Zdraveva Petranka; Yotova Maya; Kaloyanov Kaloyan; Pencheva Ivanka. Antimicrobial Peptides with Plant Origin. Int. J. Nutr. Food Sci. 2016, 5(6-1), 5-9. doi: 10.11648/j.ijnfs.s.2016050601.12

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    AMA Style

    Zdraveva Petranka, Yotova Maya, Kaloyanov Kaloyan, Pencheva Ivanka. Antimicrobial Peptides with Plant Origin. Int J Nutr Food Sci. 2016;5(6-1):5-9. doi: 10.11648/j.ijnfs.s.2016050601.12

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  • @article{10.11648/j.ijnfs.s.2016050601.12,
      author = {Zdraveva Petranka and Yotova Maya and Kaloyanov Kaloyan and Pencheva Ivanka},
      title = {Antimicrobial Peptides with Plant Origin},
      journal = {International Journal of Nutrition and Food Sciences},
      volume = {5},
      number = {6-1},
      pages = {5-9},
      doi = {10.11648/j.ijnfs.s.2016050601.12},
      url = {https://doi.org/10.11648/j.ijnfs.s.2016050601.12},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijnfs.s.2016050601.12},
      abstract = {According to the World Health Organization plants are one of the best sources to obtain a huge variety of biologically active compounds. Human population during centuries has used plants and plants extracts in ethno medicine to cure wide range of diseases. In the scope of modern methods of isolation and purification of different plant substances, antimicrobial peptides (AMPs) give us the opportunity to have a new ally in the fight with different microbial pathogens. Possible future uses of AMPs derived from plants could be either as a new class of anti-infective medications or as bio-preservatives in foods and beverages.},
     year = {2016}
    }
    

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    AU  - Zdraveva Petranka
    AU  - Yotova Maya
    AU  - Kaloyanov Kaloyan
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    AB  - According to the World Health Organization plants are one of the best sources to obtain a huge variety of biologically active compounds. Human population during centuries has used plants and plants extracts in ethno medicine to cure wide range of diseases. In the scope of modern methods of isolation and purification of different plant substances, antimicrobial peptides (AMPs) give us the opportunity to have a new ally in the fight with different microbial pathogens. Possible future uses of AMPs derived from plants could be either as a new class of anti-infective medications or as bio-preservatives in foods and beverages.
    VL  - 5
    IS  - 6-1
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Author Information
  • Department of Pharmacognosy, Faculty of Pharmacy, Medical University of Sofia, Sofia, Bulgaria

  • Medical College, Medical University of Pleven, Pleven, Bulgaria

  • Department of Pharmacology, Pharmacotherapy and Toxicology, Faculty of Pharmacy, Medical University of Sofia, Sofia, Bulgaria

  • Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Medical University of Sofia, Sofia, Bulgaria

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