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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Diaz-Roa, Andrea [1, 2, 3] ; Espinoza-Culupu, Abraham [1, 4] ; Torres-Garcia, Orlando [5] ; Borges, Monamaris M. [4] ; Avino, Ivan N. [6] ; Alves, Flavio L. [7] ; Miranda, Antonio [7] ; Patarroyo, Manuel A. [8, 9] ; da Silva, Jr., Pedro I. [1, 2] ; Bello, Felio J. [10]
Total Authors: 10
Affiliation:
[1] Univ Sao Paulo, Inst Biomed Sci, BR-05508900 Sao Paulo, SP - Brazil
[2] Butantan Inst, Special Lab Appl Toxinol LETA, BR-05503900 Sao Paulo, SP - Brazil
[3] Univ Rosario, PhD Program Biomed & Biol Sci, Bogota 111221 - Colombia
[4] Butantan Inst, Bacteriol Lab, BR-05503900 Sao Paulo, SP - Brazil
[5] Univ Antonio Narino, Med Fac, Bogota 110231 - Colombia
[6] Butantan Inst, Special Lab Cell Cycle LECC, BR-05503900 Sao Paulo, SP - Brazil
[7] Univ Fed Sao Paulo, Biophys Dept, BR-04023062 Sao Paulo - Brazil
[8] Fdn Inst Inmunol Colombia FIDIC, Mol Biol & Immunol Dept, Bogota 111321 - Colombia
[9] Univ Rosario, Sch Med & Hlth Sci, Basic Sci Dept, Bogota 112111 - Colombia
[10] Univ La Salle, Fac Agr & Livestock Sci, Vet Med Programme, Bogota 110141 - Colombia
Total Affiliations: 10
Document type: Journal article
Source: Molecules; v. 24, n. 11 JUN 1 2019.
Web of Science Citations: 1
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 M 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. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC