Morphological variation of Philodryas patagoniensis (Girard, 1858) (Serpentes, Dipsadidae) from Brazil, based on the study of pholidosis, coloration and morphometric features

Gouveia, Rafaella Vallim; Novelli, Iara Alves; Vieira, Fabiano Matos; Sousa, Bernadete Maria de

doi:10.1590/1676-0611-bn-2016-0237

Cited by 3 publications

(1 citation statement)

References 39 publications

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“…Philodryas patagoniensis is an opisthoglyphous snake, a member of the family Dipsadidae ( Utkin, 2015 ). These snakes are distributed around all South America, inhabiting different environments, and they show high plasticity when adapting to places altered by man in addition to having an excellent ability to camouflage themselves due to their coloration ( de Medeiros et al, 2010 ; Gouveia et al, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

Patagonin-CRISP: Antimicrobial Activity and Source of Antimicrobial Molecules in Duvernoy’s Gland Secretion (Philodryas patagoniensis Snake)

et al. 2021

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Snake venom contains a variety of toxins with a range of biological activity, among these toxins cysteine-rich secreted proteins (CRISPs) can be found. The proteins of this family have masses of 20–30 kDa and display homologous amino acid sequences containing 16 cysteine residues, forming eight disulfide bonds. Some of these proteins have been explored, characterized, and described in terms of their activity; however, little is known about their range of activities. A search for new antimicrobial molecules is ongoing, as the number of microbial strains resistant to available antibiotics is increasing. We identified antimicrobial activity in the secretion of Duvernoy's gland of the rear-fanged Philodryas patagoniensis. Fractions of this venom were subjected to reverse-phase high performance liquid chromatography and analyzed to determine their antimicrobial activity with a liquid broth inhibition assay. One of the fractions presented activity against a Gram-negative bacterium and a filamentous fungus. This fraction was analyzed with LC-MS/MS, and a protein of 24,848.8 Da was identified. Database searches allowed us to identify it as a CRISP due to the presence of some unique fragments in the molecule. We called it patagonin-CRISP, as the same protein in the venom of P. patagoniensis had previously been characterized as having a different biological activity. Patagonin-CRISP presented activity at very low concentrations and showed no cytotoxic activity. This is the first time that antimicrobial activity has been identified for P. patagoniensis venom or for a CRISP family protein.

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Section: Introductionmentioning

confidence: 99%

Patagonin-CRISP: Antimicrobial Activity and Source of Antimicrobial Molecules in Duvernoy’s Gland Secretion (Philodryas patagoniensis Snake)

et al. 2021

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Doderlin: isolation and characterization of a broad-spectrum antimicrobial peptide from Lactobacillus acidophilus

Silva

Díaz-Roa

Yamane

et al. 2023

Research in Microbiology

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Doderlin: Isolation and Characterization of a Broad-Spectrum Antimicrobial Peptide from Lactobacillus acidophilus

Silva

Díaz-Roa

Yamane

et al. 2022

Preprint

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Lactobacillus acidophilus are Gram-positive bacteria distributed in diverse environments, and as being a component of the normal microbiota of gastrointestinal and urogenital tract, being relevant to humans. Classified as lactic acid bacteria, due to the pro-duction of lactic acid, Lactobacillus can also produce antimicrobial peptides (AMPs), which is a compound synthesized by all forms of life aiming for protecting themselves from threats and to increase their competitivity to survive in a specific environment. AMPs are molecules capable of inhibiting the growth of microorganisms and, due to the indiscriminate use of conventional antibiotics and the emergence of multi-resistant bacteria, they have become an alternative, not only for treating multi-resistant infections, but also for probiotic product confection and food conservation. Considering the rampant rise of resistance, the present study aimed to isolate and characterize antimicrobial peptides from Lactobacillus acidophilus extracts. Samples were obtained from Lactobacillus acid extract supernatant which was pre-fractionated on disposable cartridges, followed by a high-performance liquid chromatography (HPLC). The collected fractions were evaluated in a liquid growth inhibition assay where eight fractions antimicrobial activity were obtained. One of them was selected for further characterization by mass spectrometry (MS), due to its antimicrobial activity against Candida albicans and conclusive results in mass spectrometry analysis. This molecule was identified as a peptide having a molecular mass of 1788.01 Da, peptide sequence NEPTHLLKAFSKAGFQ, and named Doderlin. Interestingly, antimicrobial molecules isolated from L. acidophilus have already been described previously, but few reports in the literature describe an AMP effective against C. 34 albicans as reported here. The results obtained suggest that this newly discovered molecule have a biological property with potential to be applied in pharmaceutical and food companies in the fight against contamination and/or for treating infections caused by microorganisms.

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Morphological variation of Philodryas patagoniensis (Girard, 1858) (Serpentes, Dipsadidae) from Brazil, based on the study of pholidosis, coloration and morphometric features

Cited by 3 publications

References 39 publications

Patagonin-CRISP: Antimicrobial Activity and Source of Antimicrobial Molecules in Duvernoy’s Gland Secretion (Philodryas patagoniensis Snake)

Patagonin-CRISP: Antimicrobial Activity and Source of Antimicrobial Molecules in Duvernoy’s Gland Secretion (Philodryas patagoniensis Snake)

Doderlin: isolation and characterization of a broad-spectrum antimicrobial peptide from Lactobacillus acidophilus

Doderlin: Isolation and Characterization of a Broad-Spectrum Antimicrobial Peptide from Lactobacillus acidophilus

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