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Antimycobacterial Activity of a New Peptide Polydim-I Isolated from Neotropical Social Wasp Polybia dimorpha.

ABSTRACT: Mycobacterium abscessus subsp. massiliense, a rapidly growing mycobacteria (RGM) that is becoming increasingly important among human infectious diseases, is virulent and pathogenic 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 antimycobacterial 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.

SUBMITTER: das Neves RC

PROVIDER: S-EPMC4773228 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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Antimycobacterial Activity of a New Peptide Polydim-I Isolated from Neotropical Social Wasp Polybia dimorpha.

das Neves Rogerio Coutinho RC Trentini Monalisa Martins MM de Castro e Silva Juliana J Simon Karina Smidt KS Bocca Anamelia Lorenzetti AL Silva Luciano Paulino LP Mortari Marcia Renata MR Kipnis Andre A Junqueira-Kipnis Ana Paula AP

PloS one 20160301 3

Mycobacterium abscessus subsp. massiliense, a rapidly growing mycobacteria (RGM) that is becoming increasingly important among human infectious diseases, is virulent and pathogenic 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 bio ...[more]

PMID: 26930596

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Project description:Background Between 9.3 and 28.5% of world population are estimated to be allergic to the protein components of Hymenoptera venom and among them, the hyaluronidase (HYAL) is one of the most important, although the nature of its IgE binding epitopes is unknown. Methods Enzyme was purified from P. paulista venom by cation exchange chromatography in AKTA-FPLC system with a Hiprep CM FF column. Fractions with HYAL activity were pooled, lyophilized, dialyzed against distilled water in presence of protease inhibitor (PMSF) and subjected to SDS-PAGE 15%. The only protein bands visualized were submitted to tryptic digestion and to MALDI-ToF/ToF mass spectrometry. Digested peptides produced were compared with partial/complete protein sequences from Data Bank including with the HYAL (Q9U6V9) of Polistes annularis venom used as model. Western blotting was performed with Pp-HYAL-specific antibody to test the identity of pure protein. Results All analysis performed identified the pure protein as an HYAL present in P.paulista venom, which also had its cDNA sequence (GI:302201582) cloned and determined in previous studies, being its high similarity with the Polistes annularis enzyme already confirmed. The mature allergenic protein has 338 amino acids and a molecular weight of 39 KDa. The same allergen is known in other insects, venoms and immunological cross reactivity may sometimes be observed among closely related species. Here, the immunoblotting assay revealed that the Pp-HYAL-specific antibody used recognized the correspondent protein in the purified fraction and in the crude venom of P. paulista, but not in the Apis mellifera and Solenopsis invicta venoms. Conclusions The methodology used was able to purify the allergen, which is a key step in the characterization of its binding epitopes. Such knowledge has direct implications in accuracy of diagnostic procedures and strategies for specific immunotherapy of allergic patients to the venom of this insect. Funding: Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP).

Dataset Information

Antimycobacterial Activity of a New Peptide Polydim-I Isolated from Neotropical Social Wasp Polybia dimorpha.

Publications

Antimycobacterial Activity of a New Peptide Polydim-I Isolated from Neotropical Social Wasp Polybia dimorpha.

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