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Pablo Victor Mendes Dos Reis
Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil

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Journal article
Published: 02 June 2020 in Current Protein & Peptide Science
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Antimicrobial peptides (AMPs) have been found in all organism taxa and may play an essential role as a host defense system. AMPs are organized in various conformations, such as linear peptides, disulfide bond-linked peptides, backbone-linked peptides and circular peptides. AMPs apparently act primarily on the plasma membrane, although an increasing number of works have shown that they may also target various intracellular sites. Spider venoms are rich sources of biomolecules that show several activities, including modulation or blockage of ion channels, anti-insect, anti-cancer, antihypertensive and antimicrobial activities, among others. In spider venoms from the Lycosidae family there are many linear AMPs with a wide range of activities against several microorganisms. Due to these singular activities, some Lycosidae AMPs have been modified to improve or decrease desirable or undesirable effects, respectively. Such modifications, especially with the aim of increasing their antibiotic activity, have led to the filing of many patent applications. This review explores the abundance of Lycosidae venom AMPs and some of their derivatives, and their use as new drug models.

ACS Style

Marcella Nunes Melo-Braga; Flávia De Marco Almeida; Daniel Moreira Dos Santos; Joaquim Teixeira De Avelar Júnior; Pablo Victor Mendes Dos Reis; Maria Elena De Lima. Antimicrobial Peptides From Lycosidae (Sundevall, 1833) Spiders. Current Protein & Peptide Science 2020, 21, 527 -541.

AMA Style

Marcella Nunes Melo-Braga, Flávia De Marco Almeida, Daniel Moreira Dos Santos, Joaquim Teixeira De Avelar Júnior, Pablo Victor Mendes Dos Reis, Maria Elena De Lima. Antimicrobial Peptides From Lycosidae (Sundevall, 1833) Spiders. Current Protein & Peptide Science. 2020; 21 (5):527-541.

Chicago/Turabian Style

Marcella Nunes Melo-Braga; Flávia De Marco Almeida; Daniel Moreira Dos Santos; Joaquim Teixeira De Avelar Júnior; Pablo Victor Mendes Dos Reis; Maria Elena De Lima. 2020. "Antimicrobial Peptides From Lycosidae (Sundevall, 1833) Spiders." Current Protein & Peptide Science 21, no. 5: 527-541.

Journal article
Published: 04 April 2019 in Toxins
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Bacterial keratitis is an ocular infection that can lead to severe visual disability. Staphylococcus aureus is a major pathogen of the eye. We recently demonstrated the strong antimicrobial activity of LyeTxI-b, a synthetic peptide derived from a Lycosa erithrognatha toxin. Herein, we evaluated a topical formulation (eye drops) containing LyeTxI-b to treat resistant bacterial keratitis. Keratitis was induced with intrastromal injection of 4 × 105 cells (4 µL) in New Zealand female white rabbits. Minimum inhibitory concentration (MIC) and biofilm viability were determined. LyeTxI-b ocular toxicity was evaluated through chorioallantoic membrane and Draize tests. One drop of the formulation (LyeTxI-b 28.9 µmol/L +0.5% CMC in 0.9% NaCl) was instilled into each eye four times a day, for a week. Slit-lamp biomicroscopy analysis, corneal histopathological studies and cellular infiltrate quantification through myeloperoxidase (MPO) and N-acetylglucosaminidase (NAG) detection were performed. LyeTxI-b was very effective in the treatment of keratitis, with no signs of ocular toxicity. Planktonic bacteria MIC was 3.6 µmol/L and LyeTxI-b treatment reduced biofilm viability in 90%. LyeTxI-b eliminated bacteria and reduced inflammatory cellular activity in the eyes. Healthy and treated animals showed similar NAG and MPO levels. LyeTxI-b is a potent new drug to treat resistant bacterial keratitis, showing effective antimicrobial and anti-inflammatory activity.

ACS Style

Carolina Nunes Da Silva; Flavia Rodrigues Da Silva; Lays Fernanda Nunes Dourado; Pablo Victor Mendes Dos Reis; Rummenigge Oliveira Silva; Bruna Lopes Da Costa; Paula Santos Nunes; Flávio Almeida Amaral; Vera Lúcia Dos Santos; Maria Elena De Lima; Armando Da Silva Cunha Júnior. A New Topical Eye Drop Containing LyeTxI-b, A Synthetic Peptide Designed from A Lycosa erithrognata Venom Toxin, Was Effective to Treat Resistant Bacterial Keratitis. Toxins 2019, 11, 203 .

AMA Style

Carolina Nunes Da Silva, Flavia Rodrigues Da Silva, Lays Fernanda Nunes Dourado, Pablo Victor Mendes Dos Reis, Rummenigge Oliveira Silva, Bruna Lopes Da Costa, Paula Santos Nunes, Flávio Almeida Amaral, Vera Lúcia Dos Santos, Maria Elena De Lima, Armando Da Silva Cunha Júnior. A New Topical Eye Drop Containing LyeTxI-b, A Synthetic Peptide Designed from A Lycosa erithrognata Venom Toxin, Was Effective to Treat Resistant Bacterial Keratitis. Toxins. 2019; 11 (4):203.

Chicago/Turabian Style

Carolina Nunes Da Silva; Flavia Rodrigues Da Silva; Lays Fernanda Nunes Dourado; Pablo Victor Mendes Dos Reis; Rummenigge Oliveira Silva; Bruna Lopes Da Costa; Paula Santos Nunes; Flávio Almeida Amaral; Vera Lúcia Dos Santos; Maria Elena De Lima; Armando Da Silva Cunha Júnior. 2019. "A New Topical Eye Drop Containing LyeTxI-b, A Synthetic Peptide Designed from A Lycosa erithrognata Venom Toxin, Was Effective to Treat Resistant Bacterial Keratitis." Toxins 11, no. 4: 203.

Original article
Published: 17 November 2018 in Amino Acids
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Antimicrobial peptides present a broad spectrum of therapeutic applications, including their use as anticancer peptides. These peptides have as target microbial, normal, and cancerous cells. The oncological properties of these peptides may occur by membranolytic mechanisms or non-membranolytics. In this work, we demonstrate for the first time the cytotoxic effects of the cationic alpha-helical antimicrobial peptide LyeTx I-b on glioblastoma lineage U87-MG. The anticancer property of this peptide was associated with a membranolytic mechanism. Loss of membrane integrity occurred after incubation with the peptide for 15 min, as shown by trypan blue uptake, reduction of calcein-AM conversion, and LDH release. Morphological studies using scanning electron microscopy demonstrated disruption of the plasma membrane from cells treated with LyeTx I-b, including the formation of holes or pores. Transmission electron microscopy analyses showed swollen nuclei with mild DNA condensation, cell volume increase with an electron-lucent cytoplasm and organelle vacuolization, but without the rupture of nuclear or plasmatic membranes. Morphometric analyses revealed a high percentage of cells in necroptosis stages, followed by necrosis and apoptosis at lower levels. Necrostatin-1, a known inhibitor of necroptosis, partially protected the cells from the toxicity of the peptide in a concentration-dependent manner. Imaging flow cytometry confirmed that 59% of the cells underwent necroptosis after 3-h incubation with the peptide. It is noteworthy that LyeTx I-b showed only mild cytotoxicity against normal fibroblasts of human and monkey cell lines and low hemolytic activity in human erythrocytes. All data together point out the anticancer potential of this peptide.

ACS Style

Mostafa A. L. Abdel-Salam; Juliana Carvalho-Tavares; Kamila Sousa Gomes; Andrea Teixeira-Carvalho; Gregory T. Kitten; Johanna Nyffeler; Felipe Ferraz Dias; Pablo V. Mendes Dos Reis; Adriano M. C. Pimenta; Marcel Leist; Maria Elena De Lima; Elaine Maria De Souza-Fagundes. The synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells. Amino Acids 2018, 51, 433 -449.

AMA Style

Mostafa A. L. Abdel-Salam, Juliana Carvalho-Tavares, Kamila Sousa Gomes, Andrea Teixeira-Carvalho, Gregory T. Kitten, Johanna Nyffeler, Felipe Ferraz Dias, Pablo V. Mendes Dos Reis, Adriano M. C. Pimenta, Marcel Leist, Maria Elena De Lima, Elaine Maria De Souza-Fagundes. The synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells. Amino Acids. 2018; 51 (3):433-449.

Chicago/Turabian Style

Mostafa A. L. Abdel-Salam; Juliana Carvalho-Tavares; Kamila Sousa Gomes; Andrea Teixeira-Carvalho; Gregory T. Kitten; Johanna Nyffeler; Felipe Ferraz Dias; Pablo V. Mendes Dos Reis; Adriano M. C. Pimenta; Marcel Leist; Maria Elena De Lima; Elaine Maria De Souza-Fagundes. 2018. "The synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells." Amino Acids 51, no. 3: 433-449.

Original research article
Published: 06 April 2018 in Frontiers in Microbiology
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The antimicrobial peptide LyeTxI isolated from the venom of the spider Lycosa erythrognatha is a potential model to develop new antibiotics against bacteria and fungi. In this work, we studied a peptide derived from LyeTxI, named LyeTxI-b, and characterized its structural profile and its in vitro and in vivo antimicrobial activities. Compared to LyeTxI, LyeTxI-b has an acetylated N-terminal and a deletion of a His residue, as structural modifications. The secondary structure of LyeTxI-b is a well-defined helical segment, from the second amino acid to the amidated C-terminal, with no clear partition between hydrophobic and hydrophilic faces. Moreover, LyeTxI-b shows a potent antimicrobial activity against Gram-positive and Gram-negative planktonic bacteria, being 10-fold more active than the native peptide against Escherichia coli. LyeTxI-b was also active in an in vivo model of septic arthritis, reducing the number of bacteria load, the migration of immune cells, the level of IL-1β cytokine and CXCL1 chemokine, as well as preventing cartilage damage. Our results show that LyeTxI-b is a potential therapeutic model for the development of new antibiotics against Gram-positive and Gram-negative bacteria.

ACS Style

Pablo V. M. Reis; Daiane Boff; Rodrigo Verly; Marcella N. Melo-Braga; Maria Esperanza Cortés; Daniel M. Santos; Adriano M. De C. Pimenta; Flávio A. Amaral; Jarbas Resende; Maria E. De Lima. LyeTxI-b, a Synthetic Peptide Derived From Lycosa erythrognatha Spider Venom, Shows Potent Antibiotic Activity in Vitro and in Vivo. Frontiers in Microbiology 2018, 9, 667 .

AMA Style

Pablo V. M. Reis, Daiane Boff, Rodrigo Verly, Marcella N. Melo-Braga, Maria Esperanza Cortés, Daniel M. Santos, Adriano M. De C. Pimenta, Flávio A. Amaral, Jarbas Resende, Maria E. De Lima. LyeTxI-b, a Synthetic Peptide Derived From Lycosa erythrognatha Spider Venom, Shows Potent Antibiotic Activity in Vitro and in Vivo. Frontiers in Microbiology. 2018; 9 ():667.

Chicago/Turabian Style

Pablo V. M. Reis; Daiane Boff; Rodrigo Verly; Marcella N. Melo-Braga; Maria Esperanza Cortés; Daniel M. Santos; Adriano M. De C. Pimenta; Flávio A. Amaral; Jarbas Resende; Maria E. De Lima. 2018. "LyeTxI-b, a Synthetic Peptide Derived From Lycosa erythrognatha Spider Venom, Shows Potent Antibiotic Activity in Vitro and in Vivo." Frontiers in Microbiology 9, no. : 667.

Journal article
Published: 27 February 2017 in Toxins
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Scorpions are among the oldest venomous living organisms and the family Buthidae is the largest and most medically relevant one. Scorpion venoms include many toxic peptides, but recently, a metalloprotease from Tityus serrulatus called antarease was reported to be capable of cleaving VAMP2, a protein involved in the neuroparalytic syndromes of tetanus and botulism. We have produced antarease and an inactive metalloprotease mutant in a recombinant form and analyzed their enzymatic activity on recombinant VAMP2 in vitro and on mammalian and insect neuromuscular junction. The purified recombinant antarease paralyzed the neuromuscular junctions of mice and of Drosophila melanogaster whilst the mutant was inactive. We were unable to demonstrate any cleavage of VAMP2 under conditions which leads to VAMP proteolysis by botulinum neurotoxin type B. Antarease caused a reduced release probability, mainly due to defects upstream of the synaptic vesicles fusion process. Paired pulse experiments indicate that antarease might proteolytically inactivate a voltage-gated calcium channel.

ACS Style

Irene Zornetta; Michele Scorzeto; Pablo Victor Mendes Dos Reis; Maria E. De Lima; Cesare Montecucco; Aram Megighian; Ornella Rossetto. Electrophysiological Characterization of the Antarease Metalloprotease from Tityus serrulatus Venom. Toxins 2017, 9, 81 .

AMA Style

Irene Zornetta, Michele Scorzeto, Pablo Victor Mendes Dos Reis, Maria E. De Lima, Cesare Montecucco, Aram Megighian, Ornella Rossetto. Electrophysiological Characterization of the Antarease Metalloprotease from Tityus serrulatus Venom. Toxins. 2017; 9 (3):81.

Chicago/Turabian Style

Irene Zornetta; Michele Scorzeto; Pablo Victor Mendes Dos Reis; Maria E. De Lima; Cesare Montecucco; Aram Megighian; Ornella Rossetto. 2017. "Electrophysiological Characterization of the Antarease Metalloprotease from Tityus serrulatus Venom." Toxins 9, no. 3: 81.

Journal article
Published: 19 January 2017 in Journal of Venomous Animals and Toxins including Tropical Diseases
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The availability of antimicrobial peptides from several different natural sources has opened an avenue for the discovery of new biologically active molecules. To the best of our knowledge, only two peptides isolated from the frog Leptodactylus labyrinthicus, namely pentadactylin and ocellatin-F1, have shown antimicrobial activities. Therefore, in order to explore the antimicrobial potential of this species, we have investigated the biological activities and membrane interactions of three peptides isolated from the anuran skin secretion. Three peptide primary structures were determined by automated Edman degradation. These sequences were prepared by solid-phase synthesis and submitted to activity assays against gram-positive and gram-negative bacteria and against two fungal strains. The hemolytic properties of the peptides were also investigated in assays with rabbit blood erythrocytes. The conformational preferences of the peptides and their membrane interactions have been investigated by circular dichroism spectroscopy and liposome dye release assays. The amino acid compositions of three ocellatins were determined and the sequences exhibit 100% homology for the first 22 residues (ocellatin-LB1 sequence). Ocellatin-LB2 carries an extra Asn residue and ocellatin-F1 extra Asn-Lys-Leu residues at C-terminus. Ocellatin-F1 presents a stronger antibiotic potential and a broader spectrum of activities compared to the other peptides. The membrane interactions and pore formation capacities of the peptides correlate directly with their antimicrobial activities, i.e., ocellatin-F1 > ocellatin-LB1 > ocellatin-LB2. All peptides acquire high helical contents in membrane environments. However, ocellatin-F1 shows in average stronger helical propensities. The obtained results indicate that the three extra amino acid residues at the ocellatin-F1 C-terminus play an important role in promoting stronger peptide-membrane interactions and antimicrobial properties. The extra Asn-23 residue present in ocellatin-LB2 sequence seems to decrease its antimicrobial potential and the strength of the peptide-membrane interactions.

ACS Style

Karla A. G. Gusmão; Daniel M. Dos Santos; Virgílio M. Santos; María Esperanza Cortés; Pablo V. M. Reis; Vera L. Santos; Dorila Piló-Veloso; Rodrigo M. Verly; Maria Elena De Lima; Jarbas M. Resende. Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions. Journal of Venomous Animals and Toxins including Tropical Diseases 2017, 23, 1 -14.

AMA Style

Karla A. G. Gusmão, Daniel M. Dos Santos, Virgílio M. Santos, María Esperanza Cortés, Pablo V. M. Reis, Vera L. Santos, Dorila Piló-Veloso, Rodrigo M. Verly, Maria Elena De Lima, Jarbas M. Resende. Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions. Journal of Venomous Animals and Toxins including Tropical Diseases. 2017; 23 (1):1-14.

Chicago/Turabian Style

Karla A. G. Gusmão; Daniel M. Dos Santos; Virgílio M. Santos; María Esperanza Cortés; Pablo V. M. Reis; Vera L. Santos; Dorila Piló-Veloso; Rodrigo M. Verly; Maria Elena De Lima; Jarbas M. Resende. 2017. "Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions." Journal of Venomous Animals and Toxins including Tropical Diseases 23, no. 1: 1-14.

Book chapter
Published: 14 September 2015 in Spider Venoms
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Historically, toxinologists have regarded venom studies focusing on lethality and other apparent toxic effects using mammals and insects as models. Nevertheless, with the development of sensitive and accessible analytical techniques, novel structures, especially peptides lacking observable effects in mammal and insect systems, have been increasingly noticed. Among such novel structures and activities are the antimicrobial peptides (AMPs). In this chapter, we review the current literature dealing with AMPs from spider venoms since their first appearance back in 1998, when a peptide was isolated from the venom of a species of wolf spider. It is also worth mentioning that the description of such peptides is constantly expanding, along with the information gathered regarding their structure and functional relationships over the last decade.

ACS Style

Daniel M. Santos; Pablo. V. Reis; Adriano M. C. Pimenta. Antimicrobial Peptides in Spider Venoms. Spider Venoms 2015, 1 -15.

AMA Style

Daniel M. Santos, Pablo. V. Reis, Adriano M. C. Pimenta. Antimicrobial Peptides in Spider Venoms. Spider Venoms. 2015; ():1-15.

Chicago/Turabian Style

Daniel M. Santos; Pablo. V. Reis; Adriano M. C. Pimenta. 2015. "Antimicrobial Peptides in Spider Venoms." Spider Venoms , no. : 1-15.