Antimicrobial peptidomes of Bothrops atrox and Bothrops jararacussu snake venoms.
Autor: | da Silva Caldeira CA; Center for the Study of Biomolecules Applied to Health (CEBio), Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Porto Velho, RO, Brazil. cleopatra@unir.br.; Graduate Program in Biodiversity and Biotechnology, BIONORTE Network, Porto Velho, RO, Brazil. cleopatra@unir.br.; Graduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO, Brazil. cleopatra@unir.br., Diniz-Sousa R; Center for the Study of Biomolecules Applied to Health (CEBio), Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Porto Velho, RO, Brazil.; Graduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO, Brazil.; São Lucas University Center (UniSL), Porto Velho, RO, Brazil., Pimenta DC; Biochemistry and Biophysics Laboratory, Butantan Institute, Sao Paulo, SP, Brazil., Dos Santos APA; Graduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO, Brazil.; Malaria and Leishmaniasis Bioassay Platform, PBML, Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Porto Velho, RO, Brazil., Teles CBG; Graduate Program in Biodiversity and Biotechnology, BIONORTE Network, Porto Velho, RO, Brazil.; Graduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO, Brazil.; São Lucas University Center (UniSL), Porto Velho, RO, Brazil.; Malaria and Leishmaniasis Bioassay Platform, PBML, Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Porto Velho, RO, Brazil., Matos NB; Microbiology Laboratory, Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Research Center on Tropical Medicine of Rondônia (CEPEM), Porto Velho, RO, Brazil., da Silva SL; College of Biochemistry and Pharmacy, Faculty of Chemical Sciences, University of Cuenca, Cuenca, Azuay, Ecuador.; Chemistry and Biochemistry Department, Faculty of Sciences, University of Porto, Porto, Portugal.; LAQV - REQUIMTE, University of Porto, Porto, Portugal., Stabeli RG; Translational Medicine Platform, Fiocruz, Ribeirão Preto, São Paulo, Brazil.; Faculty of Medicine of the Federal University of São Carlos (UFSCAR), São Paulo, Brazil., Camperi SA; Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Cátedra de Biotecnología, Buenos Aires, Argentina.; CONICET-Universidad de Buenos Aires, Instituto de Nanobiotecnología (NANOBIOTEC), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina., Soares AM; Center for the Study of Biomolecules Applied to Health (CEBio), Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Porto Velho, RO, Brazil.; Graduate Program in Biodiversity and Biotechnology, BIONORTE Network, Porto Velho, RO, Brazil.; Graduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO, Brazil.; São Lucas University Center (UniSL), Porto Velho, RO, Brazil., de Azevedo Calderon L; Center for the Study of Biomolecules Applied to Health (CEBio), Oswaldo Cruz Foundation Rondônia, FIOCRUZ, Porto Velho, RO, Brazil. calderon@unir.br.; Graduate Program in Biodiversity and Biotechnology, BIONORTE Network, Porto Velho, RO, Brazil. calderon@unir.br.; Graduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO, Brazil. calderon@unir.br.; Aparício Carvalho University Center (FIMCA), Porto Velho, RO, Brazil. calderon@unir.br. |
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Jazyk: | angličtina |
Zdroj: | Amino acids [Amino Acids] 2021 Oct; Vol. 53 (10), pp. 1635-1648. Date of Electronic Publication: 2021 Sep 04. |
DOI: | 10.1007/s00726-021-03055-y |
Abstrakt: | The worrisome emergence of pathogens resistant to conventional drugs has stimulated the search for new classes of antimicrobial and antiparasitic agents from natural sources. Antimicrobial peptides (AMPs), acting through mechanisms that do not rely on the interaction with a specific receptor, provide new possibilities for the development of drugs against resistant organisms. This study sought to purify and proteomically characterize the antimicrobial and antiparasitic peptidomes of B. atrox and B. jararacussu snake venoms against Gram-positive (Staphylococcus aureus, Methicillin-resistant Staphylococcus aureus-MRSA), Gram-negative (Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae) bacteria, and the protozoan parasites Leishmania amazonensis and Plasmodium falciparum (clone W2, resistant to chloroquine). To this end, B. atrox and B. jararacussu venom peptides were purified by combination of 3 kDa cut-off Amicon ® ultracentrifugal filters and reverse-phase high-performance liquid chromatography, and then identified by electrospray-ionization Ion-Trap/Time-of-Flight mass spectrometry. Fourteen distinct peptides, with masses ranging from 443.17 to 1383.73 Da and primary structure between 3 and 13 amino acid residues, were sequenced. Among them, 13 contained unique sequences, including 4 novel bradykinin-potentiating-like peptides (BPPs), and a snake venom metalloproteinase tripeptide inhibitor (SVMPi). Although commonly found in Viperidae venoms, except for Bax-12, the BPPs and SVMPi here reported had not been described in B. atrox and B. jararacussu venoms. Among the novel peptides, some exhibited bactericidal activity towards P. aeruginosa and S. aureus, had low hemolytic effect, and were devoid of antiparasitic activity. The identified novel antimicrobial peptides may be relevant in the development of new drugs for the management of multidrug-resistant Gram-negative and Gram-positive bacteria. (© 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.) |
Databáze: | MEDLINE |
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