Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)

Larval therapy (LT) is an alternative treatment which uses fly larvae to heal chronic wounds; its action is based on debridement, bacterial removal and stimulating granulation tissue. The most important mechanism for fighting infection with LT depends on larval excretions and secretions (ES). The la...

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Fecha de publicación:
2019
Institución:
Universidad del Rosario
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Repositorio EdocUR - U. Rosario
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eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/20460
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https://doi.org/10.48713/10336_20460
https://repository.urosario.edu.co/handle/10336/20460
Palabra clave:
Antimicrobial peptide
Larval therapy
Sarconesiopsis magellanica
Ciencias médicas, Medicina
Medicina
Peptidos
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id EDOCUR2_81fb1f7e67ce609d2e62ba9b0384ca4e
oai_identifier_str oai:repository.urosario.edu.co:10336/20460
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
dc.title.spa.fl_str_mv Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
title Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
spellingShingle Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
Antimicrobial peptide
Larval therapy
Sarconesiopsis magellanica
Ciencias médicas, Medicina
Medicina
Peptidos
title_short Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
title_full Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
title_fullStr Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
title_full_unstemmed Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
title_sort Isolating and characterizing antimicrobial peptides derived from larvae of the blowfly Sarconesiopsis magellanica (diptera: Calliphoridae)
dc.contributor.advisor.none.fl_str_mv Bello García, Felio Jesús
da Silva Junior, Pedro Ismael
Patarroyo, Manuel A.
dc.subject.spa.fl_str_mv Antimicrobial peptide
Larval therapy
Sarconesiopsis magellanica
topic Antimicrobial peptide
Larval therapy
Sarconesiopsis magellanica
Ciencias médicas, Medicina
Medicina
Peptidos
dc.subject.ddc.spa.fl_str_mv Ciencias médicas, Medicina
dc.subject.lemb.spa.fl_str_mv Medicina
Peptidos
description Larval therapy (LT) is an alternative treatment which uses fly larvae to heal chronic wounds; its action is based on debridement, bacterial removal and stimulating granulation tissue. The most important mechanism for fighting infection with LT depends on larval excretions and secretions (ES). The larvae are protected by an antimicrobial peptide (1) spectrum. Sarconesiopsis magellanica is a promising necrophagous fly for use in medicine. This study was thus aimed at identifying and characterizing S. magellanica AMPs contained in ES, for the first time. ES were fractionated by RP-HPLC using C18 columns. The products were lyophilized, and their antimicrobial activity characterized. The sequences were determined by mass spectrometry. The mechanism of action was evaluated by fluorescence and electronic microscopy. Toxicity was tested on HeLA cells and human erythrocytes; the physicochemical properties of the identified peptides were evaluated. Two molecules in the ES were characterized: sarconesin (a new peptide having antibacterial activity against Gram-negative (Escherichia coli D31, Pseudomonas aeruginosa 27853) and Gram-positive (Staphylococcus aureus ATCC 29213, Micrococcus luteus A270) bacteria and sarconsesin II, having activity against Gram-negative (E. coli MG1655, P. aeruginosa ATCC 27853) and Gram-positive (S. aureus ATCC 29213, M. luteus A270) bacteria. The minimum inhibitory concentrations ranged from 1.2 μM upwards; the AMPs did not have toxicity in any tested cells and their action on bacterial membrane and DNA was confirmed. Sarconesin had similarity with the CDC42 protein belonging to the Rho-family of GTPases which are important in organelle development and wound repair. Sarconesin II was seen to be a conserved domain of the ATP synthase protein belonging to the FliI superfamily. The data reported here indicates that the peptides could be alternative therapeutic candidates for use in infections against Gram-negative and Gram-positive microorganisms and as new resources to combat resistance against antimicrobial agents.
publishDate 2019
dc.date.accessioned.none.fl_str_mv 2019-10-18T16:50:35Z
dc.date.available.none.fl_str_mv 2019-10-18T16:50:35Z
dc.date.created.none.fl_str_mv 2019-08-28
dc.type.eng.fl_str_mv doctoralThesis
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_db06
dc.type.document.spa.fl_str_mv Tesis
dc.type.spa.spa.fl_str_mv Tesis de doctorado
dc.identifier.doi.none.fl_str_mv https://doi.org/10.48713/10336_20460
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/20460
url https://doi.org/10.48713/10336_20460
https://repository.urosario.edu.co/handle/10336/20460
dc.language.iso.spa.fl_str_mv eng
language eng
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.acceso.spa.fl_str_mv Abierto (Texto Completo)
rights_invalid_str_mv Abierto (Texto Completo)
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Universidad del Rosario
dc.publisher.department.spa.fl_str_mv Facultad de Ciencias Naturales y Matemáticas
dc.publisher.program.spa.fl_str_mv Doctorado en Ciencias Biomédicas y Biológicas
institution Universidad del Rosario
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spelling Bello García, Felio Jesús8103f4e0-e43d-4cb8-add2-a559ca1f5b47600da Silva Junior, Pedro Ismael7f0281c9-70d4-4bb4-bb53-fa283ded6e65-1Patarroyo, Manuel A.79653065600Díaz Roa, AndreaDoctor en Ciencias Biomédicas y BiológicasFull timebe5e3bfd-0002-4551-8df5-71f3e76905dc6002019-10-18T16:50:35Z2019-10-18T16:50:35Z2019-08-28Larval therapy (LT) is an alternative treatment which uses fly larvae to heal chronic wounds; its action is based on debridement, bacterial removal and stimulating granulation tissue. The most important mechanism for fighting infection with LT depends on larval excretions and secretions (ES). The larvae are protected by an antimicrobial peptide (1) spectrum. Sarconesiopsis magellanica is a promising necrophagous fly for use in medicine. This study was thus aimed at identifying and characterizing S. magellanica AMPs contained in ES, for the first time. ES were fractionated by RP-HPLC using C18 columns. The products were lyophilized, and their antimicrobial activity characterized. The sequences were determined by mass spectrometry. The mechanism of action was evaluated by fluorescence and electronic microscopy. Toxicity was tested on HeLA cells and human erythrocytes; the physicochemical properties of the identified peptides were evaluated. Two molecules in the ES were characterized: sarconesin (a new peptide having antibacterial activity against Gram-negative (Escherichia coli D31, Pseudomonas aeruginosa 27853) and Gram-positive (Staphylococcus aureus ATCC 29213, Micrococcus luteus A270) bacteria and sarconsesin II, having activity against Gram-negative (E. coli MG1655, P. aeruginosa ATCC 27853) and Gram-positive (S. aureus ATCC 29213, M. luteus A270) bacteria. The minimum inhibitory concentrations ranged from 1.2 μM upwards; the AMPs did not have toxicity in any tested cells and their action on bacterial membrane and DNA was confirmed. Sarconesin had similarity with the CDC42 protein belonging to the Rho-family of GTPases which are important in organelle development and wound repair. Sarconesin II was seen to be a conserved domain of the ATP synthase protein belonging to the FliI superfamily. The data reported here indicates that the peptides could be alternative therapeutic candidates for use in infections against Gram-negative and Gram-positive microorganisms and as new resources to combat resistance against antimicrobial agents.ColcienciasButantan Instituteapplication/pdfhttps://doi.org/10.48713/10336_20460 https://repository.urosario.edu.co/handle/10336/20460engUniversidad del RosarioFacultad de Ciencias Naturales y MatemáticasDoctorado en Ciencias Biomédicas y BiológicasAbierto (Texto Completo)PARGRAFO: En caso de presentarse cualquier reclamación o acción por parte de un tercero en cuanto a los derechos de autor sobre la obra en cuestión, EL AUTOR, asumirá toda la responsabilidad, y saldrá en defensa de los derechos aquí autorizados; para todos los efectos la universidad actúa como un tercero de buena fe.http://purl.org/coar/access_right/c_abf21. Classamp. 2019 [March 7th 2019]. Available from: http://www.bicnirrh.res.in/classamp/predict.php.2. 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