The potential of Loxosceles gaucho spider venom to regulate Pseudomonas aeruginosa mechanisms of virulence

Domingos, Marta de Oliveira; Neves, Irys Viana; Vigerelli, Hugo; Pimenta, Daniel C.; Távora, Bianca de Carvalho Lins Fernandes; Lemos, Thiago Jordão; Franzolin, Márcia Regina; Marques, Vaniky Duarte; Barbaro, Kátia Cristina

doi:10.1016/j.toxicon.2018.07.017

Cited by 8 publications

(6 citation statements)

References 32 publications

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“…However, so far there is only one report that indicates that L. gaucho venom contains low-molecular-mass molecules with antimicrobial activity against Pseudomonas aeruginosa . The study also mentions that the whole venom of this spider does not influence the proliferation of P. aeruginosa , but increases its biofilm formation, as well as the production of gelatinase and caseinase [55].…”

Section: Resultsmentioning

confidence: 99%

Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

Segura-Ramírez

Júnior

2018

Toxins

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The remarkable ability of microorganisms to develop resistance to conventional antibiotics is one of the biggest challenges that the pharmaceutical industry currently faces. Recent studies suggest that antimicrobial peptides discovered in spider venoms may be useful resources for the design of structurally new anti-infective agents effective against drug-resistant microorganisms. In this work, we found an anionic antibacterial peptide named U1-SCRTX-Lg1a in the venom of the spider Loxosceles gaucho. The peptide was purified using high-performance liquid chromatography (HPLC), its antimicrobial activity was tested through liquid growth inhibition assays, and its chemical properties were characterized using mass spectrometry. U1-SCRTX-Lg1a was found to show a monoisotopic mass of 1695.75 Da, activity against Gram-negative bacteria, a lack of hemolytic effects against human red blood cells, and a lack of cytotoxicity against human cervical carcinoma cells (HeLa). Besides this, the sequence of the peptide exhibited great similarity to specific regions of phospholipases D from different species of Loxosceles spiders, leading to the hypothesis that U1-SCRTX-Lg1a may have originated from a limited proteolytic cleavage. Our data suggest that U1-SCRTX-Lg1a is a promising candidate for the development of new antibiotics that could help fight bacterial infections and represents an exciting discovery for Loxosceles spiders.

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Section: Resultsmentioning

confidence: 99%

Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

Segura-Ramírez

Júnior

2018

Toxins

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“…Venom components responsible for this antimicrobial activity were also investigated. This includes acylpolyamines, such as the polyamine toxin VdTX-I from Vitalius dubius [22], and low molecular mass molecules, such as those extracted from Laxosceles spider, which affected the virulence of Pseudomonas aeruginosa strains [23]. Many other antimicrobial peptides were identified from spider venom.…”

Section: Antimicrobial Agents From Spidersmentioning

confidence: 99%

Antimicrobials from Venomous Animals: An Overview

et al. 2020

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The inappropriate or excessive use of antimicrobial agents caused an emerging public health problem due to the resulting resistance developed by microbes. Therefore, there is an urgent need to develop effective antimicrobial strategies relying on natural agents with different mechanisms of action. Nature has been known to offer many bioactive compounds, in the form of animal venoms, algae, and plant extracts that were used for decades in traditional medicine. Animal venoms and secretions have been deeply studied for their wealth in pharmaceutically promising molecules. As such, they were reported to exhibit many biological activities of interest, such as antibacterial, antiviral, anticancer, and anti-inflammatory activities. In this review, we summarize recent findings on the antimicrobial activities of crude animal venoms/secretions, and describe the peptides that are responsible of these activities.

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“…Arthropod venoms are natural sources of a wide spectrum of biologically active molecules, including neurotoxic, hemolytic, antiarrhythmic, anticonvulsant, antitumoral, anti-inflammatory, antimicrobial, and insecticidal agents among others. − Targets of these molecules can be receptors, ion channels, enzymes, or other proteins in cells that may play critical roles in homeostasis. Therefore, venom-derived molecules represent a prominent repository of drug-lead candidates …”

Section: Introductionmentioning

confidence: 99%

“…Therefore, venom-derived molecules represent a prominent repository of drug-lead candidates. 5 Molecular complexity of venoms is in part attributed to protein post-translational modifications (PTMs). Proteolysis is an overlooked PTM in the field that generates a myriad of cryptic peptides (also known as cryptides) from native toxins.…”

Section: ■ Introductionmentioning

confidence: 99%

Moving Pieces in a Cellular Puzzle: A Cryptic Peptide from the Scorpion Toxin Ts14 Activates AKT and ERK Signaling and Decreases Cardiac Myocyte Contractility via Dephosphorylation of Phospholamban

et al. 2020

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Cryptic peptides (cryptides) are biologically active peptides formed after proteolysis of native precursors present in animal venoms, for example. Proteolysis is an overlooked post-translational modification (PTM) that increases venom complexity.The tripeptide KPP (Lys-Pro-Pro) is a peptide encrypted in the C-terminus of Ts14a 25-mer peptide from the venom of Tityus serrulatus scorpion that has a positive impact on the cardiovascular system, inducing vasodilation and reducing arterial blood pressure of hypertensive rats, among other beneficial effects. A previous study reported that KPP and its native peptide Ts14 act via activation of the bradykinin receptor B2 (B2R). However, the cellular events underlying the activation of B2R by KPP are unknown. To study the cell signaling triggered by the Ts14 cryptide KPP, we incubated cardiac myocytes isolated from C57BL/6 mice with KPP (10 -7 mol.L -1 ) for 0 min, 5 min or 30 min and explored the proteome and phosphoproteome. Our results showed that KPP regulated cardiomyocyte proteins associated with, but not limited to, apoptosis, muscle contraction, protein turnover, and the respiratory chain.We also reported that KPP led to AKT phosphorylation, activating AKT and its downstream target eNOS. We also observed that KPP led to dephosphorylation of phospholamban (PLN) at its activation sites (S16 and T17) leading to reduced contractility of treated cardiomyocytes. Some cellular targets reported here for KPP (e.g., AKT, PLN and ERK) have already been reported to protect cardiac tissue of hypoxia-induced injury. Hence, this study suggests potential beneficial effects of this scorpion cryptide that needs to be further investigated, for example as a drug lead for cardiac infarction.

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The potential of Loxosceles gaucho spider venom to regulate Pseudomonas aeruginosa mechanisms of virulence

Cited by 8 publications

References 32 publications

Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

Antimicrobials from Venomous Animals: An Overview

Moving Pieces in a Cellular Puzzle: A Cryptic Peptide from the Scorpion Toxin Ts14 Activates AKT and ERK Signaling and Decreases Cardiac Myocyte Contractility via Dephosphorylation of Phospholamban

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