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Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions.
Molecules. 2019 May 31; 24(11)M

Abstract

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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Authors+Show Affiliations

Díaz-Roa A
Special Laboratory for Applied Toxinology (LETA), Butantan Institute, São Paulo CEP 05503-900, SP, Brazil. andreadiazroa186@gmail.com. Institute of Biomedical Sciences, University of São Paulo, São Paulo CEP 05508-900, SP, Brazil. andreadiazroa186@gmail.com. PhD Program in Biomedical and Biological Sciences, Universidad del Rosario, Bogotá 111221, Colombia. andreadiazroa186@gmail.com.
Espinoza-Culupú A
Institute of Biomedical Sciences, University of São Paulo, São Paulo CEP 05508-900, SP, Brazil. abraham.culupu@butantan.gov.br. Bacteriology Laboratory, Butantan Institute, São Paulo CEP 05503-900, SP, Brazil. abraham.culupu@butantan.gov.br.
Torres-García O
Medicine Faculty, Universidad Antonio Nariño, Bogotá 110231, Colombia. ortorres@uan.edu.co.
Borges MM
Bacteriology Laboratory, Butantan Institute, São Paulo CEP 05503-900, SP, Brazil. monamaris.borges@butantan.gov.br.
Avino IN
Special Laboratory of Cell Cycle (LECC), Butantan Institute, São Paulo CEP 05503-900, SP, Brazil. ivan.avino@butantan.gov.br.
Alves FL
Biophysics Department, UNIFESP, São Paulo CEP 04023-062, Brazil. pelopes2@yahoo.com.br.
Miranda A
Biophysics Department, UNIFESP, São Paulo CEP 04023-062, Brazil. amiranda@unifesp.br.
Patarroyo MA
Molecular Biology and Immunology Department, Fundación Instituto de Inmunología de Colombia (FIDIC), Bogotá 111321, Colombia. mapatarr.fidic@gmail.com. Basic Sciences Department, School of Medicine and Health Sciences, Universidad del Rosario, Bogotá 112111, Colombia. mapatarr.fidic@gmail.com.
da Silva PI
Special Laboratory for Applied Toxinology (LETA), Butantan Institute, São Paulo CEP 05503-900, SP, Brazil. pedro.junior@butantan.gov.br. Institute of Biomedical Sciences, University of São Paulo, São Paulo CEP 05508-900, SP, Brazil. pedro.junior@butantan.gov.br.
Bello FJ
Faculty of Agricultural and Livestock Sciences, Veterinary Medicine Programme, Universidad de La Salle, Bogotá 110141, Colombia. fbgarcia5@yahoo.es.

MeSH

Amino Acid SequenceAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriaChemical PhenomenaChromatography, High Pressure LiquidDipteraDose-Response Relationship, DrugMass SpectrometryMicrobial Sensitivity TestsModels, MolecularProtein ConformationStructure-Activity Relationship

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31159162

Citation

Díaz-Roa, Andrea, et al. "Sarconesin II, a New Antimicrobial Peptide Isolated From Sarconesiopsis Magellanica Excretions and Secretions." Molecules (Basel, Switzerland), vol. 24, no. 11, 2019.
Díaz-Roa A, Espinoza-Culupú A, Torres-García O, et al. Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions. Molecules. 2019;24(11).
Díaz-Roa, A., Espinoza-Culupú, A., Torres-García, O., Borges, M. M., Avino, I. N., Alves, F. L., Miranda, A., Patarroyo, M. A., da Silva, P. I., & Bello, F. J. (2019). Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions. Molecules (Basel, Switzerland), 24(11). https://doi.org/10.3390/molecules24112077
Díaz-Roa A, et al. Sarconesin II, a New Antimicrobial Peptide Isolated From Sarconesiopsis Magellanica Excretions and Secretions. Molecules. 2019 May 31;24(11) PubMed PMID: 31159162.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sarconesin II, a New Antimicrobial Peptide Isolated from Sarconesiopsis magellanica Excretions and Secretions. AU - Díaz-Roa,Andrea, AU - Espinoza-Culupú,Abraham, AU - Torres-García,Orlando, AU - Borges,Monamaris M, AU - Avino,Ivan N, AU - Alves,Flávio L, AU - Miranda,Antonio, AU - Patarroyo,Manuel A, AU - da Silva,Pedro I,Jr AU - Bello,Felio J, Y1 - 2019/05/31/ PY - 2019/03/09/received PY - 2019/04/11/revised PY - 2019/04/20/accepted PY - 2019/6/5/entrez PY - 2019/6/5/pubmed PY - 2019/11/26/medline KW - Calliphoridae KW - Sarconesiopsis magellanica KW - alpha-helix KW - antimicrobial peptide KW - drug JF - Molecules (Basel, Switzerland) JO - Molecules VL - 24 IS - 11 N2 - 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. SN - 1420-3049 UR - https://www.unboundmedicine.com/medline/citation/31159162/Sarconesin_II_a_New_Antimicrobial_Peptide_Isolated_from_Sarconesiopsis_magellanica_Excretions_and_Secretions_ DB - PRIME DP - Unbound Medicine ER -