Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

Segura-Ramírez, Paula J.; Júnior, Pedro I Silva

doi:10.3390/toxins10120522

Cited by 25 publications

(15 citation statements)

References 75 publications

(99 reference statements)

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“…Eight two-fold serial dilutions of sarconesin II were evaluated at 100 µM final concentration and incubated for 1 h at 37 °C. Hemolytic activity was determined by measuring absorbance (Abs) at 405 nm and calculated as a percentage of 100% lysis control (0.1% Triton X-100); % hemolysis = (Abs sample–negative Abs)/(positive Abs − negative Abs) [137].…”

Section: Methodsmentioning

confidence: 99%

“…MS/MS peak list files were screened against a bank database constructed with the Lucilia proteins obtained from UNIPROT and NCBI [138,139] to determine their aa sequence. They were compared using PEAKS 8.5 (Bioinformatics Solutions Inc., Waterloo, ON, Canada) search software, using the following parameters: oxidation considered as variable modification, 10 ppm precursor mass tolerance and 0.6 fragment ion mass tolerance [137].…”

Section: Methodsmentioning

confidence: 99%

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Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

et al. 2019

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Antibiotic resistance is at dangerous levels and increasing worldwide. The search for new antimicrobial drugs to counteract this problem is a priority for health institutions and organizations, both globally and in individual countries. Sarconesiopsis magellanica blowfly larval excretions and secretions (ES) are an important source for isolating antimicrobial peptides (AMPs). This study aims to identify and characterize a new S. magellanica AMP. RP-HPLC was used to fractionate ES, using C18 columns, and their antimicrobial activity was evaluated. The peptide sequence of the fraction collected at 43.7 min was determined by mass spectrometry (MS). Fluorescence and electronic microscopy were used to evaluate the mechanism of action. Toxicity was tested on HeLa cells and human erythrocytes; physicochemical properties were evaluated. The molecule in the ES was characterized as sarconesin II and it showed activity against Gram-negative (Escherichia coli MG1655, Pseudomonas aeruginosa ATCC 27853, P. aeruginosa PA14) and Gram-positive (Staphylococcus aureus ATCC 29213, Micrococcus luteus A270) bacteria. The lowest minimum inhibitory concentration obtained was 1.9 μM for M. luteus A270; the AMP had no toxicity in any cells tested here and its action in bacterial membrane and DNA was confirmed. Sarconesin II was documented as a conserved domain of the ATP synthase protein belonging to the Fli-1 superfamily. The data reported here indicated that peptides could be alternative therapeutic candidates for use in infections against Gram-negative and Gram-positive bacteria and eventually as a new resource of compounds for combating multidrug-resistant bacteria.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

et al. 2019

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“…Interestingly, an antimicrobial peptide (1695.75 Da), recently identified in L. gaucho venom, presented a remarkable similarity to specific regions of phospholipases D from Loxosceles genus. This peptide, referred to as U1-SCRTX-Lg1a, possesses an antibacterial effect on gram-negative bacteria [11]. The authors suggested that U1-SCRTX-Lg1a may have originated by limited proteolysis of a venom PLD.…”

Section: Molecular Characteristics Of Brown Spider Venomsmentioning

confidence: 99%

Forty Years of the Description of Brown Spider Venom Phospholipases-D

Gremski

Justa

Silva

et al. 2020

Toxins

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Spiders of the genus Loxosceles, popularly known as Brown spiders, are considered a serious public health issue, especially in regions of hot or temperate climates, such as parts of North and South America. Although the venoms of these arachnids are complex in molecular composition, often containing proteins with distinct biochemical characteristics, the literature has primarily described a family of toxins, the Phospholipases-D (PLDs), which are highly conserved in all Loxosceles species. PLDs trigger most of the major clinical symptoms of loxoscelism i.e., dermonecrosis, thrombocytopenia, hemolysis, and acute renal failure. The key role played by PLDs in the symptomatology of loxoscelism was first described 40 years ago, when researches purified a hemolytic toxin that cleaved sphingomyelin and generated choline, and was referred to as a Sphingomyelinase-D, which was subsequently changed to Phospholipase-D when it was demonstrated that the enzyme also cleaved other cellular phospholipids. In this review, we present the information gleaned over the last 40 years about PLDs from Loxosceles venoms especially with regard to the production and characterization of recombinant isoforms. The history of obtaining these toxins is discussed, as well as their molecular organization and mechanisms of interaction with their substrates. We will address cellular biology aspects of these toxins and how they can be used in the development of drugs to address inflammatory processes and loxoscelism. Present and future aspects of loxoscelism diagnosis will be discussed, as well as their biotechnological applications and actions expected for the future in this field.

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“…Antimicrobial peptides and proteins show a wide distribution and have been isolated from nearly all living organisms. [8][9][10][11][12][13][14][15][16][17][18][19][20][21] Beyond their antimicrobial effects, several AMPs have been shown to have other biological activities. 11,[22][23][24][25] One such protein group that represents the duplicity of activities for the same molecules is the tachykinin family.…”

Section: Introductionmentioning

confidence: 99%

“…Antimicrobial peptides and proteins show a wide distribution and have been isolated from nearly all living organisms. 8 - 21 …”

Section: Introductionmentioning

confidence: 99%

Two Tachykinin-Related Peptides with Antimicrobial Activity Isolated from Triatoma infestans Hemolymph

et al. 2020

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Antimicrobial peptides and proteins (AMPs) are molecules that can interact with microbial cells and lead to membrane disruption or intracellular molecule interactions and death. Several molecules with antimicrobial effects also present other biological activities. One such protein group representing the duplicity of activities is the tachykinin family. Tachykinins (TKs) form a family of neuropeptides in vertebrates with a consensus C-terminal region (F-X-G-Y-R-NH2). Invertebrate TKs and TK-related peptides (TKRPs) are subfamilies found in invertebrates that present high homology with TKs and have similar biological effects. Several of these molecules have already been described but reports of TKRP in Hemiptera species are limited. By analyzing the Triatoma infestans hemolymph by reversed-phase high-performance liquid chromatography, biological assays, and mass spectrometry, two antimicrobial molecules were isolated and identified as TKRPs, which we named as TRP1-TINF and TRP2-TINF (tachykinin-related peptides I and II from T. infestans). TRP1-TINF is a random secondary structure peptide with 9 amino acid residues. It is susceptible to aminopeptidases degradation and is active mainly against Micrococcus luteus (32 μM). TRP2-TINF is a 10-amino acid peptide with a 310 helix secondary structure and is susceptible to carboxypeptidases degradation. It has major antimicrobial activity against both Pseudomonas aeruginosa and Escherichia coli (45 μM). Neither molecule is toxic to human erythrocytes and both present minor toxicity toward Vero cells at a concentration of 1000 μM. As the first description of TKRPs with antimicrobial activity in T. infestans, this work contributes to the wider comprehension of the insects’ physiology and describes pharmacological relevant molecules.

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Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

Cited by 25 publications

References 75 publications

Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions

Forty Years of the Description of Brown Spider Venom Phospholipases-D

Two Tachykinin-Related Peptides with Antimicrobial Activity Isolated from Triatoma infestans Hemolymph

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