Biological Production of Antimicrobial Peptides Against Plants as Well as Human Pathogens

2020 ◽  
Vol 13 (2) ◽  
pp. 410-423
Author(s):  
Farwa Basit
Keyword(s):  
Antimicrobial Peptides ◽  
Human Pathogens ◽  
Biological Production

Antimicrobial Peptides: Phylogenic Sources and Biological Activities. First of Two Parts

2018 ◽  
Vol 24 (10) ◽  
pp. 1043-1053 ◽  
Author(s):  
Thea Magrone ◽  
Matteo Antonio Russo ◽  
Emilio Jirillo
Keyword(s):  
Antimicrobial Peptides ◽  
Biological Activities ◽  
Cell Types ◽  
Human Pathogens ◽  
New Class ◽  
Novel Drugs ◽  
Broad Variety ◽  
Living Organisms ◽  
Self Protection

Antimicrobial peptides (AMPs) are phylogenetically ancient substances released by living organisms for self protection against a broad variety of microbes. Moreover, AMPs are endowed with immune modulatory activities, linking innate and adaptive immunity together. Lantibiotics are AMPs of bacterial origin currently investigated for the generation of a new class of anti-infective compounds, owing to the phenomenon of antibiotic resistance against a broad variety of bacteria. Also, plants and marine AMPs are screened as novel drugs against human pathogens. Human AMPs encompass defensins and cathelicidins produced by various cell types mostly at mucosal sites. Besides their antimicrobial activity, both AMPs have been shown to trigger either inflammatory or anti-inflammatory pathways. Food-derived AMPs are mostly represented by lactoferrin and lysozyme both present in secretions, e.g., milk, and appear to be very exploitable for the generation of functional foods. Finally, the role of natural products ingested with food or administered as supplements on induction and production of AMPs will be discussed.

scholarly journals Towards improved resistance of Corynebacterium glutamicum against nisin

2021 ◽  
Author(s):  
Dominik Weixler ◽  
Oliver Goldbeck ◽  
Gerd Michael Seibold ◽  
Bernhard Johannes Eikmanns ◽  
Christian Ullrich Riedel
Keyword(s):  
Antimicrobial Peptides ◽  
Corynebacterium Glutamicum ◽  
Cell Envelope ◽  
Resistance Mechanisms ◽  
Heterologous Production ◽  
Human Pathogens ◽  
Gram Positive Bacteria ◽  
Lipid Ii ◽  
Immunity Genes ◽  
Abc Transporter Genes

The bacteriocin nisin is one of the best studied antimicrobial peptides. It is widely used as a food preservative due to its antimicrobial activity against various Gram-positive bacteria including human pathogens such as Listeria monocytogenes and others. The receptor of nisin is the universal cell wall precursor lipid II, which is present in all bacteria. Thus, nisin has a broad spectrum of target organisms. Consequently, heterologous production of nisin with biotechnological relevant organisms including Corynebacterium glutamicum is difficult. Nevertheless, bacteria have evolved several mechanisms of resistance against nisin and other cationic antimicrobial peptides (CAMPs). Here, we transferred resistance mechanisms described in other organisms to C. glutamicum with the aim to improve nisin resistance. The presented approaches included: expression of (i) nisin immunity genes nisI and/or nisFEG or (ii) nisin ABC-transporter genes of Staphylococcus aureus and its homologues of C. glutamicum, (iii) genes coding for enzymes for alanylation or lysinylation of the cell envelope to introduce positive charges, and/or (iv) deletion of genes for porins of the outer membrane. None of the attempts alone increased resistance of C. glutamicum more than two-fold. To increase resistance of C. glutamicum to levels that will allow heterologous production of active nisin at relevant titers, further studies are needed.

scholarly journals One pathogen two stones: are Australian tree frog antimicrobial peptides synergistic against human pathogens?

2017 ◽  
Vol 46 (7) ◽  
pp. 639-646 ◽  
Author(s):  
Marc-Antoine Sani ◽  
Siobhan Carne ◽  
Sarah A. Overall ◽  
Alexandre Poulhazan ◽  
Frances Separovic
Keyword(s):  
Antimicrobial Peptides ◽  
Tree Frog ◽  
Human Pathogens

scholarly journals New Antibacterial Peptides from the Freshwater Mollusk Pomacea poeyana (Pilsbry, 1927)

Biomolecules ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1473
Author(s):  
Melaine González García ◽  
Armando Rodríguez ◽  
Annia Alba ◽  
Antonio A. Vázquez ◽  
Fidel E. Morales Vicente ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Galleria Mellonella ◽  
Random Coil ◽  
Helical Conformation ◽  
Moderate Activity ◽  
Human Pathogens ◽  
Spectra Analysis ◽  
Bacterial Membranes ◽  
Innate Defense

Antimicrobial peptides (AMPs) are biomolecules with antimicrobial activity against a broad group of pathogens. In the past few decades, AMPs have represented an important alternative for the treatment of infectious diseases. Their isolation from natural sources has been widely investigated. In this sense, mollusks are promising organisms for the identification of AMPs given that their immune system mainly relies on innate response. In this report, we characterized the peptide fraction of the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) and identified 37 different peptides by nanoLC-ESI-MS-MS technology. From these peptide sequences, using bioinformatic prediction tools, we discovered two potential antimicrobial peptides named Pom-1 (KCAGSIAWAIGSGLFGGAKLIKIKKYIAELGGLQ) and Pom-2 (KEIERAGQRIRDAIISAAPAVETLAQAQKIIKGG). Database search revealed that Pom-1 is a fragment of Closticin 574 previously isolated from the bacteria Clostridium tyrobutyrium, and Pom-2 is a fragment of cecropin D-like peptide first isolated from Galleria mellonella hemolymph. These sequences were chemically synthesized and evaluated against different human pathogens. Interestingly, structural predictions of both peptides in the presence of micelles showed models that comprise two alpha helices joined by a short loop. The CD spectra analysis of Pom-1 and Pom-2 in water showed for both structures a high random coil content, a certain content of α-helix and a low β-sheet content. Like other described AMPs displaying a disordered structure in water, the peptides may adopt a helical conformation in presence of bacterial membranes. In antimicrobial assays, Pom-1 demonstrated high activity against the Gram-negative bacteria Pseudomonas aeruginosa and moderate activity against Klebsiella pneumoniae and Listeria monocytogenes. Neither of the two peptides showed antifungal action. Pom-1 moderately inhibits Zika Virus infection but slightly enhances HIV-1 infectivion in vitro. The evaluation of cell toxicity on primary human macrophages did not show toxicity on THP-1 cells, although slight overall toxicity was observed in high concentrations of Pom-1. We assume that both peptides may play a key role in innate defense of P. poeyana and represent promising antimicrobial candidates for humans.

scholarly journals Diversity, evolution and medical applications of insect antimicrobial peptides

2016 ◽  
Vol 371 (1695) ◽  
pp. 20150290 ◽  
Author(s):  
Eleftherios Mylonakis ◽  
Lars Podsiadlowski ◽  
Maged Muhammed ◽  
Andreas Vilcinskas
Keyword(s):  
Antimicrobial Peptides ◽  
High Throughput Screening ◽  
Rational Design ◽  
Evolutionary Ecology ◽  
Multidrug Resistant ◽  
Screening Methods ◽  
Medical Applications ◽  
Human Pathogens ◽  
Acinetobacter Baumanii ◽  
Multidrug Resistant Pathogens

Antimicrobial peptides (AMPs) are short proteins with antimicrobial activity. A large portion of known AMPs originate from insects, and the number and diversity of these molecules in different species varies considerably. Insect AMPs represent a potential source of alternative antibiotics to address the limitation of current antibiotics, which has been caused by the emergence and spread of multidrug-resistant pathogens. To get more insight into AMPs, we investigated the diversity and evolution of insect AMPs by mapping their phylogenetic distribution, allowing us to predict the evolutionary origins of selected AMP families and to identify evolutionarily conserved and taxon-specific families. Furthermore, we highlight the use of the nematode Caenorhabditis elegans as a whole-animal model in high-throughput screening methods to identify AMPs with efficacy against human pathogens, including Acinetobacter baumanii and methicillin-resistant Staphylococcus aureus . We also discuss the potential medical applications of AMPs, including their use as alternatives for conventional antibiotics in ectopic therapies, their combined use with antibiotics to restore the susceptibility of multidrug-resistant pathogens, and their use as templates for the rational design of peptidomimetic drugs that overcome the disadvantages of therapeutic peptides. The article is part of the themed issue ‘Evolutionary ecology of arthropod antimicrobial peptides’.

scholarly journals Design and characterization of chionodracine-derived antimicrobial peptides with enhanced activity against drug-resistant human pathogens

RSC Advances ◽  
2018 ◽  
Vol 8 (72) ◽  
pp. 41331-41346 ◽  
Author(s):  
Cristina Olivieri ◽  
Francesca Bugli ◽  
Giulia Menchinelli ◽  
Gianluigi Veglia ◽  
Francesco Buonocore ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Drug Resistant ◽  
Human Pathogens ◽  
Enhanced Activity

Design of new chionodracine-derived peptides with potent activity against drug-resistant human pathogens.

scholarly journals Zn-Enhanced Asp-Rich Antimicrobial Peptides: N-Terminal Coordination by Zn(II) and Cu(II), which Distinguishes Cu(II) Binding to Different Peptides

2021 ◽  
Vol 22 (13) ◽  
pp. 6971
Author(s):  
Adriana Miller ◽  
Agnieszka Matera-Witkiewicz ◽  
Aleksandra Mikołajczyk ◽  
Joanna Wątły ◽  
Dean Wilcox ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Metal Ions ◽  
Epr Spectroscopy ◽  
Pulmonary Surfactant ◽  
Mannheimia Haemolytica ◽  
Lewis Acidity ◽  
Human Pathogens ◽  
Square Planar ◽  
Entropically Driven

The antimicrobial activity of surfactant-associated anionic peptides (SAAPs), which are isolated from the ovine pulmonary surfactant and are selective against the ovine pathogen Mannheimia haemolytica, is strongly enhanced in the presence of Zn(II) ions. Both calorimetry and ITC measurements show that the unique Asp-only peptide SAAP3 (DDDDDDD) and its analogs SAAP2 (GDDDDDD) and SAAP6 (GADDDDD) have a similar micromolar affinity for Zn(II), which binds to the N-terminal amine and Asp carboxylates in a net entropically-driven process. All three peptides also bind Cu(II) with a net entropically-driven process but with higher affinity than they bind Zn(II) and coordination that involves the N-terminal amine and deprotonated amides as the pH increases. The parent SAAP3 binds Cu(II) with the highest affinity; however, as shown with potentiometry and absorption, CD and EPR spectroscopy, Asp residues in the first and/or second positions distinguish Cu(II) binding to SAAP3 and SAAP2 from their binding to SAAP6, decreasing the Cu(II) Lewis acidity and suppressing its square planar amide coordination by two pH units. We also show that these metal ions do not stabilize a membrane disrupting ability nor do they induce the antimicrobial activity of these peptides against a panel of human pathogens.

scholarly journals In Vitro Evaluation of Antimicrobial Peptides from the Black Soldier Fly ( Hermetia Illucens ) against a Selection of Human Pathogens

2022 ◽  
Author(s):  
Laurence Van Moll ◽  
Jeroen De Smet ◽  
Anne Paas ◽  
Dorothee Tegtmeier ◽  
Andreas Vilcinskas ◽  
...  
Keyword(s):  
Antimicrobial Resistance ◽  
Drug Development ◽  
Antimicrobial Peptides ◽  
Human Pathogens ◽  
Resistance Development ◽  
Black Soldier Fly ◽  
In Vitro Evaluation ◽  
Conventional Antibiotics ◽  
Selection Of

With the ever growing antimicrobial resistance, finding new candidates for antimicrobial drug development is indispensable. Antimicrobial peptides have steadily gained attention as alternatives for conventional antibiotics, due to some highly desirable characteristics, such as their low propensity for resistance development.

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