Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles

Sayegh, Raphael Santa Rosa; Batista, Isabel de Fátima Correia; Melo, Robson L.; Riske, Karin A.; Daffre, Sirlei; Montich, Guillermo G.; Silva, Pedro Ismael da

doi:10.1371/journal.pone.0167953

Cited by 27 publications

(22 citation statements)

References 57 publications

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“…Absorbance at 550 nm was measured using a microplate ELISA reader. Cell survival was calculated using the following formula: survival (%) = (A550 of peptide-treated cells/A550 of peptide-untreated cells) ∗ 100 ( Sayegh et al, 2016 ).…”

Section: Methodsmentioning

confidence: 99%

Sarconesin: Sarconesiopsis magellanica Blowfly Larval Excretions and Secretions With Antibacterial Properties

et al. 2018

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Larval therapy (LT) is an alternative treatment for healing chronic wounds; its action is based on debridement, the removal of bacteria, and stimulating granulation tissue. The most important mechanism when using LT for combating infection depends on larval excretions and secretions (ES). Larvae are protected against infection by a spectrum of antimicrobial peptides (AMPs); special interest in AMPs has also risen regarding understanding their role in wound healing since they degrade necrotic tissue and kill different bacteria during LT. Sarconesiopsis magellanica (Diptera: Calliphoridae) is a promising medically-important necrophagous fly. This article reports a small AMP being isolated from S. magellanica ES products for the first time; these products were obtained from third-instar larvae taken from a previously-established colony. ES were fractionated by RP-HPLC using C18 columns for the first analysis; the products were then lyophilised and their antimicrobial activity was characterized by incubation with different bacterial strains. These fractions’ primary sequences were determined by mass spectrometry and de novo sequencing; five AMPs were obtained, the Sarconesin fraction was characterized and antibacterial activity was tested in different concentrations with minimum inhibitory concentrations starting at 1.2 μM. Potent inhibitory activity was shown against Gram-negative (Escherichia coli D31, E. coli DH5α, Salmonella enterica ATCC 13314, Pseudomonas aeruginosa 27853) and Gram-positive (Staphylococcus aureus ATCC 29213, S. epidermidis ATCC 12228, Micrococcus luteus A270) bacteria. Sarconesin has a significant similarity with Rho-family GTPases which are important in organelle development, cytoskeletal dynamics, cell movement, and wound repair. The data reported here indicated that Sarconesin could be an alternative candidate for use in therapeutics against Gram-negative and Gram-positive bacterial infections. Our study describes one peptide responsible for antibacterial activity when LT is being used. The results shown here support carrying out further experiments aimed at validating S. magellanica AMPs as novel resources for combating antibacterial resistance.

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Section: Methodsmentioning

confidence: 99%

Sarconesin: Sarconesiopsis magellanica Blowfly Larval Excretions and Secretions With Antibacterial Properties

et al. 2018

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“…The b-sheet structure of these amyloids can spontaneously insert into membranes, forming channels that trigger death by ion dyshomeostasis [69]. This useful property led to conservation of amyloid AMPs across broad evolutionary taxa, such as longipin in the arachnid Acutisoma longipes [70] and microcin E492 in the bacterium Klebsiella pneumoniae RYC492 [71]. A number of amyloid AMPs are known to function in humans.…”

Section: Antimicrobial Properties Of Abmentioning

confidence: 99%

Alzheimer’s Amyloid-β is an Antimicrobial Peptide: A Review of the Evidence

Gosztyla

Brothers

Robinson

2018

JAD

193

173

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The amyloid-b (Ab) peptide has long been considered to be the driving force behind Alzheimer's disease (AD). However, clinical trials that have successfully reduced Ab burden in the brain have not slowed the cognitive decline, and in some instances have resulted in adverse outcomes. While these results can be interpreted in different ways, a more nuanced picture of Ab is emerging that takes into account the facts that the peptide is evolutionarily conserved and is present throughout life in cognitively normal individuals. Recent evidence indicates a role for Ab as an antimicrobial peptide (AMP), a class of innate immune defense molecule that utilizes fibrillation to protect the host from a wide range of infectious agents. In humans and in animal models, infection of the brain frequently leads to increased amyloidogenic processing of the Ab precursor protein (AbPP) and resultant fibrillary aggregates of Ab. Evidence from in vitro and in vivo studies demonstrates that Ab oligomers have potent, broad-spectrum antimicrobial properties by forming fibrils that entrap pathogens and disrupt cell membranes. Importantly, overexpression of Ab confers increased resistance to infection from both bacteria and viruses. The antimicrobial role of Ab may explain why increased rates of infection have been observed in some of the AD clinical trials that depleted Ab. Perhaps progress towards a cure for AD will accelerate once treatment strategies begin to take into account the likely physiological functions of this enigmatic peptide.

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“…A beguiling hypothesis is that amyloidogenic peptides are antimicrobial, host‐defense peptides . In accordance with this, amyloidogenic peptides and antimicrobial peptides (AMPs) share the ability to bind to/within a cell membrane inducing a similar permeation (barrel‐stave or toroidal pores) or disruption (carpet or detergent effect) of the membrane, while doing so via potentially different mechanisms .…”

Section: Introductionmentioning

confidence: 97%

Amyloid aggregation and membrane activity of the antimicrobial peptide uperin 3.5

et al. 2018

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Amyloid fibrils are highly ordered, β‐sheet rich forms of aggregated peptides and proteins that are associated with a variety of pathological human disorders, including Alzheimer's and Parkinson's diseases. Amyloid fibril‐forming peptides may be functionally related to antimicrobial peptides, despite differing significantly in sequence and structure. Specifically, their interaction with lipid membranes has mechanistic similarities. The 17‐amino acid peptide uperin 3.5 (U3.5) from an Australian amphibian is antimicrobial and amyloidogenic. Using a quartz crystal microbalance, we investigated the interaction of U3.5 with artificial membranes and found that (i) the membrane interaction of U3.5 is independent of the peptide's aggregation state, (ii) the presence of cholesterol in the membrane dramatically alters peptide–membrane interaction leading to a transmembrane pore‐like arrangement of U3.5, and (iii) electrostatic interaction is important for the membrane activity of U3.5 whereby removal of the positive charge at position 7 of U3.5 enhanced its fibrillar aggregation and ablated its membrane interaction, i.e. there is an inverse relationship between the antimicrobial and amyloidogenic properties of U3.5.

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Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles

Cited by 27 publications

References 57 publications

Sarconesin: Sarconesiopsis magellanica Blowfly Larval Excretions and Secretions With Antibacterial Properties

Sarconesin: Sarconesiopsis magellanica Blowfly Larval Excretions and Secretions With Antibacterial Properties

Alzheimer’s Amyloid-β is an Antimicrobial Peptide: A Review of the Evidence

Amyloid aggregation and membrane activity of the antimicrobial peptide uperin 3.5

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