scholarly journals Antibacterial Activity of Plant Defensins

2019 ◽  
Vol 32 (5) ◽  
pp. 507-514 ◽  
Author(s):  
Andrew E. Sathoff ◽  
Deborah A. Samac

Plant defensins are antimicrobial host defense peptides expressed in all higher plants. Performing a significant role in plant innate immunity, plant defensins display potent activity against a wide range of pathogens. Vertebrate and invertebrate defensins have well-characterized antibacterial activity, but plant defensins are commonly considered to display antimicrobial activity against only fungi. In this review, we highlight the often-overlooked antibacterial activity of plant defensins. Also, we illustrate methods to evaluate defensins for antibacterial activity and describe the current advances in uncovering their antibacterial modes of action.

2019 ◽  
Author(s):  
Taichiro Ishige ◽  
Hiromi HARA ◽  
Takashi HIRANO ◽  
Tomohiro KONO ◽  
Kei HANZAWA

Abstract Background Japanese quail is a low-fat, meat-bird species exhibiting high disease resistance. Cathelicidins (CATHs) are host defense peptides conserved across numerous vertebrate species that play an important role in innate immunity. The activity of host defense peptides can be affected by amino acid substitutions. However, no polymorphisms in avian CATH genes have been reported to date. The aim of this study was to clarify the effect on antimicrobial activity of polymorphisms in CATHs. Results DNA for genomic analyses was extracted from the peripheral blood of 99 randomly selected quail from 6 inbred lines. A total of six, four, four, and six CjCATH3 , CjCATH2 , CjCATHB1 , and CjCATH1 alleles were identified, respectively. Nine haplotypes, including four that were strain specific, were identified in alleles from the CjCATH3 , CjCATH2 , CjCATHB1 , and CjCATH1 loci. In addition, two and one amino acid substitutions (I145F, Q148H, and P245H) predicted by PROVEAN and PolyPhen-2 to have deleterious effects were detected at CjCATH2 and B1, respectively. Synthetic CjCATH2 and B1 peptides exhibited greater antibacterial activity against Escherichia coli than chicken CATH2 and B1, respectively. Furthermore, CjCATHB1*04 peptide exhibited less-potent antimicrobial activity than other CjCATHB1 peptides examined. Conclusions This is the first report of amino acid substitutions accompanied by changes in antibacterial activity in avian CATHs. These findings could be employed as indicators of improvements in the innate immune response in poultry.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Blazej Slazak ◽  
Klara Kaltenböck ◽  
Karin Steffen ◽  
Martyna Rogala ◽  
Priscila Rodríguez-Rodríguez ◽  
...  

AbstractCyclotides are cyclic peptides produced by plants. Due to their insecticidal properties, they are thought to be involved in host defense. Violets produce complex mixtures of cyclotides, that are characteristic for each species and variable in different environments. Herein, we utilized mass spectrometry (LC–MS, MALDI-MS), transcriptomics and biological assays to investigate the diversity, differences in cyclotide expression based on species and different environment, and antimicrobial activity of cyclotides found in violets from the Canary Islands. A wide range of different habitats can be found on these islands, from subtropical forests to dry volcano peaks at high altitudes. The islands are inhabited by the endemic Viola palmensis, V. cheiranthifolia, V. anagae and the common V. odorata. The number of cyclotides produced by a given species varied in plants from different environments. The highest diversity was noted in V. anagae which resides in subtropical forest and the lowest in V. cheiranthifolia from the Teide volcano. Transcriptome sequencing and LC–MS were used to identify 23 cyclotide sequences from V. anagae. Cyclotide extracts exhibited antifungal activities with the lowest minimal inhibitory concentrations noted for V. anagae (15.62 μg/ml against Fusarium culmorum). The analysis of the relative abundance of 30 selected cyclotides revealed patterns characteristic to both species and populations, which can be the result of genetic variability or environmental conditions in different habitats. The current study exemplifies how plants tailor their host defense peptides for various habitats, and the usefulness of cyclotides as markers for chemosystematics.


2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Mireille A. Boink ◽  
Sanne Roffel ◽  
Kamran Nazmi ◽  
Jan G. M. Bolscher ◽  
Enno C. I. Veerman ◽  
...  

Even though skin and oral mucosae are continuously in contact with commensal and opportunistic microorganisms, they generally remain healthy and uninflamed. Host defense peptides (HDPs) make up the body’s first line of defense against many invading pathogens and are involved in the orchestration of innate immunity and the inflammatory response. In this study, we investigated the effect of two salivary HDPs, LL-37 and Hst1, on the inflammatory and antimicrobial response by skin and oral mucosa (gingiva) keratinocytes and fibroblasts. The potent antimicrobial chemokine CCL20 was investigated and compared with chemokines CCL2, CXCL1, CXCL8, and CCL27 and proinflammatory cytokines IL-1αand IL-6. Keratinocyte-fibroblast cocultures showed a synergistic increase in CCL20 secretion upon Hst1 and LL-37 exposure compared to monocultures. These cocultures also showed increased IL-6, CXCL1, CXCL8, and CCL2 secretion, which was IL-1αdependent. Secretion of the antimicrobial chemokine CCL20 was clearly IL-1αindependent. These results indicate that salivary peptides can stimulate skin as well as gingiva cells to secrete antimicrobial chemokines as part of the hosts’ defense to counteract infection.


2008 ◽  
Vol 22 (2) ◽  
pp. 247-265 ◽  
Author(s):  
A. Linde ◽  
C.R. Ross ◽  
E.G. Davis ◽  
L. Dib ◽  
F. Blecha ◽  
...  

2019 ◽  
Vol 20 (21) ◽  
pp. 5289 ◽  
Author(s):  
Adenrele Oludiran ◽  
David S. Courson ◽  
Malia D. Stuart ◽  
Anwar R. Radwan ◽  
John C. Poutsma ◽  
...  

The development of new therapeutic options against Clostridioides difficile (C. difficile) infection is a critical public health concern, as the causative bacterium is highly resistant to multiple classes of antibiotics. Antimicrobial host-defense peptides (HDPs) are highly effective at simultaneously modulating the immune system function and directly killing bacteria through membrane disruption and oxidative damage. The copper-binding HDPs piscidin 1 and piscidin 3 have previously shown potent antimicrobial activity against a number of Gram-negative and Gram-positive bacterial species but have never been investigated in an anaerobic environment. Synergy between piscidins and metal ions increases bacterial killing aerobically. Here, we performed growth inhibition and time-kill assays against C. difficile showing that both piscidins suppress proliferation of C. difficile by killing bacterial cells. Microscopy experiments show that the peptides accumulate at sites of membrane curvature. We find that both piscidins are effective against epidemic C. difficile strains that are highly resistant to other stresses. Notably, copper does not enhance piscidin activity against C. difficile. Thus, while antimicrobial activity of piscidin peptides is conserved in aerobic and anaerobic settings, the peptide–copper interaction depends on environmental oxygen to achieve its maximum potency. The development of pharmaceuticals from HDPs such as piscidin will necessitate consideration of oxygen levels in the targeted tissue.


Biochimie ◽  
2010 ◽  
Vol 92 (9) ◽  
pp. 1236-1241 ◽  
Author(s):  
Daisuke Takahashi ◽  
Sanjeev K. Shukla ◽  
Om Prakash ◽  
Guolong Zhang

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