Antimycobacterial activity of a new peptide Polydim-I isolated from neotropical social wasp Polybia dimorpha
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2016
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Mycobacterium abscessus subsp. massiliense, a rapidly growing mycobacteria (RGM) that
is becoming increasingly important among human infectious diseases, is virulent and patho genic and presents intrinsic resistance to several antimicrobial drugs that might hamper
their elimination. Therefore, the identification of new drugs to improve the current treatment
or lower the risk of inducing resistance is urgently needed. Wasp venom primarily comprises
peptides that are responsible for most of the biological activities in this poison. Here, a novel
peptide Polydim-I, from Polybia dimorpha Neotropical wasp, was explored as an antimyco bacterial agent. Polydim-I provoked cell wall disruption and exhibited non-cytotoxicity
towards mammalian cells. Polydim-I treatment of macrophages infected with different M.
abscessus subsp. massiliense strains reduced 40 to 50% of the bacterial load. Additionally,
the Polydim-I treatment of highly susceptible mice intravenously infected with M. abscessus
subsp. massiliense induced 0.8 to 1 log reduction of the bacterial load in the lungs, spleen,
and liver. In conclusion, this is the first study to show the therapeutic potential of a peptide
derived from wasp venom in treating mycobacteria infections. Polydim-I acts on the M.
abscessus subsp. massiliense cell wall and reduce 40–90% of the bacterial load both in
vitro and in vivo. The presented results encourage further studies on the use of Polydim-I as
one of the components for M. abscessus subsp. massiliense treatment.
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NEVES, Rogerio Coutinho das et al. Antimycobacterial activity of a new peptide Polydim-I isolated from neotropical social wasp Polybia dimorpha. Plos One, San Francisco, v. 11, n. 3, e0149729, 2016. DOI: 10.1371/journal.pone.0149729. Disponível em: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773228/. Acesso em: 22 ago. 2024.