Biological and Enzymatic Characterization of Proteases from Crude Venom of the Ant Odontomachus bauri

Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri. Its crude venom presents several protein b...

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Published in:	Toxins Vol. 7; no. 12; pp. 5114 - 5128
Main Authors:	Silva, Mariana Ferreira, Mota, Caroline Martins, Miranda, Vanessa dos Santos, Cunha, Amanda de Oliveira, Silva, Maraísa Cristina, Naves, Karinne Spirandelli Carvalho, de Oliveira, Fábio, Silva, Deise Aparecida de Oliveira, Mineo, Tiago Wilson Patriarca, Santiago, Fernanda Maria
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI 30-11-2015 MDPI AG
Subjects:	Animals Ant Venoms - enzymology Ant Venoms - toxicity Anti-Bacterial Agents - toxicity Antiparasitic Agents - toxicity Ants Cell Survival - drug effects Coagulants - toxicity crude venom Erythrocytes - drug effects Escherichia coli - drug effects Escherichia coli - genetics HeLa Cells Hemolysis Humans Insect Proteins - metabolism Macrophages - drug effects Male Mice Odontomachus bauri Peptide Hydrolases - metabolism proteases Staphylococcus aureus - drug effects Staphylococcus aureus - growth & development Toxoplasma - drug effects Toxoplasma - pathogenicity Toxoplasma gondii Toxoplasma gondii Odontomachus bauri crude venom proteases
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Abstract	Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri. Its crude venom presents several protein bands, with higher staining for six proteins with gelatinolytic activity (17, 20, 26, 29, 43 and 48 kDa). The crude venom showed high proteolytic activity on azocasein at optimal pH 8.0 and 37 °C. In the presence of protease inhibitors as aprotinin, leupeptin and EDTA, the azocaseinolytic activity was reduced by 45%, 29% and 9%, respectively, suggesting that the enzymes present in the crude venom belong to the three classes of proteases, with the serine proteases in greater intensity. The crude venom degraded the fibrinogen α-chain faster than the β-chain, while the fibrinogen γ-chain remained unchanged. In biological assays, O. bauri venom showed hemolytic and coagulant activity in vitro, and defibrinating activity in vivo. In addition, the venom showed antimicrobial activity against Staphylococcus aureus and Escherichia coli as well as antiparasitic activity on Toxoplasma gondii infection in vitro. In that sense, this study sheds perspectives for pharmacological applications of O. bauri venom enzymes.
AbstractList	Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri . Its crude venom presents several protein bands, with higher staining for six proteins with gelatinolytic activity (17, 20, 26, 29, 43 and 48 kDa). The crude venom showed high proteolytic activity on azocasein at optimal pH 8.0 and 37 °C. In the presence of protease inhibitors as aprotinin, leupeptin and EDTA, the azocaseinolytic activity was reduced by 45%, 29% and 9%, respectively, suggesting that the enzymes present in the crude venom belong to the three classes of proteases, with the serine proteases in greater intensity. The crude venom degraded the fibrinogen α-chain faster than the β-chain, while the fibrinogen γ-chain remained unchanged. In biological assays, O. bauri venom showed hemolytic and coagulant activity in vitro , and defibrinating activity in vivo . In addition, the venom showed antimicrobial activity against Staphylococcus aureus and Escherichia coli as well as antiparasitic activity on Toxoplasma gondii infection in vitro . In that sense, this study sheds perspectives for pharmacological applications of O. bauri venom enzymes. Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri. Its crude venom presents several protein bands, with higher staining for six proteins with gelatinolytic activity (17, 20, 26, 29, 43 and 48 kDa). The crude venom showed high proteolytic activity on azocasein at optimal pH 8.0 and 37 °C. In the presence of protease inhibitors as aprotinin, leupeptin and EDTA, the azocaseinolytic activity was reduced by 45%, 29% and 9%, respectively, suggesting that the enzymes present in the crude venom belong to the three classes of proteases, with the serine proteases in greater intensity. The crude venom degraded the fibrinogen α-chain faster than the β-chain, while the fibrinogen γ-chain remained unchanged. In biological assays, O. bauri venom showed hemolytic and coagulant activity in vitro, and defibrinating activity in vivo. In addition, the venom showed antimicrobial activity against Staphylococcus aureus and Escherichia coli as well as antiparasitic activity on Toxoplasma gondii infection in vitro. In that sense, this study sheds perspectives for pharmacological applications of O. bauri venom enzymes.
Author	Mota, Caroline Martins Silva, Mariana Ferreira Miranda, Vanessa dos Santos Cunha, Amanda de Oliveira de Oliveira, Fábio Naves, Karinne Spirandelli Carvalho Santiago, Fernanda Maria Silva, Maraísa Cristina Mineo, Tiago Wilson Patriarca Silva, Deise Aparecida de Oliveira
AuthorAffiliation	2 Institute of Biomedical Sciences, Laboratory of Clinical Bacteriology, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil; kscnaves@icbim.ufu.br 3 Institute of Biomedical Sciences, Laboratory of Biophysics, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil; foliveira@umuarama.ufu.br 1 Institute of Biomedical Sciences, Laboratory of Immunoparasitology “Dr. Mario Endsfeldz Camargo”, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil; marianaa_fs@hotmail.com (M.F.S.); carolinemartinsm@yahoo.com.br (C.M.M.); vanessa.smiranda@hotmail.com (V.S.M.); amanda.olicunha@hotmail.com (A.O.C.); maraisa2003@yahoo.com.br (M.C.S.); daosilva@yahoo.com.br (D.A.O.S.); tiagomineo@icbim.ufu.br (T.W.P.M.) 4 National Institute in Science and Technology in Nanobiopharmaceutics (NanoBiofar), Belo Horizonte-MG 31270-901, Brazil
AuthorAffiliation_xml	– name: 3 Institute of Biomedical Sciences, Laboratory of Biophysics, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil; foliveira@umuarama.ufu.br – name: 4 National Institute in Science and Technology in Nanobiopharmaceutics (NanoBiofar), Belo Horizonte-MG 31270-901, Brazil – name: 1 Institute of Biomedical Sciences, Laboratory of Immunoparasitology “Dr. Mario Endsfeldz Camargo”, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil; marianaa_fs@hotmail.com (M.F.S.); carolinemartinsm@yahoo.com.br (C.M.M.); vanessa.smiranda@hotmail.com (V.S.M.); amanda.olicunha@hotmail.com (A.O.C.); maraisa2003@yahoo.com.br (M.C.S.); daosilva@yahoo.com.br (D.A.O.S.); tiagomineo@icbim.ufu.br (T.W.P.M.) – name: 2 Institute of Biomedical Sciences, Laboratory of Clinical Bacteriology, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil; kscnaves@icbim.ufu.br
Author_xml	– sequence: 1 givenname: Mariana Ferreira surname: Silva fullname: Silva, Mariana Ferreira email: marianaa_fs@hotmail.com organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. marianaa_fs@hotmail.com – sequence: 2 givenname: Caroline Martins surname: Mota fullname: Mota, Caroline Martins email: carolinemartinsm@yahoo.com.br organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. carolinemartinsm@yahoo.com.br – sequence: 3 givenname: Vanessa dos Santos surname: Miranda fullname: Miranda, Vanessa dos Santos email: vanessa.smiranda@hotmail.com organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. vanessa.smiranda@hotmail.com – sequence: 4 givenname: Amanda de Oliveira surname: Cunha fullname: Cunha, Amanda de Oliveira email: amanda.olicunha@hotmail.com organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. amanda.olicunha@hotmail.com – sequence: 5 givenname: Maraísa Cristina surname: Silva fullname: Silva, Maraísa Cristina email: maraisa2003@yahoo.com.br organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. maraisa2003@yahoo.com.br – sequence: 6 givenname: Karinne Spirandelli Carvalho surname: Naves fullname: Naves, Karinne Spirandelli Carvalho email: kscnaves@icbim.ufu.br organization: Institute of Biomedical Sciences, Laboratory of Clinical Bacteriology, Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. kscnaves@icbim.ufu.br – sequence: 7 givenname: Fábio surname: de Oliveira fullname: de Oliveira, Fábio email: foliveira@umuarama.ufu.br, foliveira@umuarama.ufu.br organization: National Institute in Science and Technology in Nanobiopharmaceutics (NanoBiofar), Belo Horizonte-MG 31270-901, Brazil. foliveira@umuarama.ufu.br – sequence: 8 givenname: Deise Aparecida de Oliveira surname: Silva fullname: Silva, Deise Aparecida de Oliveira email: daosilva@yahoo.com.br organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. daosilva@yahoo.com.br – sequence: 9 givenname: Tiago Wilson Patriarca surname: Mineo fullname: Mineo, Tiago Wilson Patriarca email: tiagomineo@icbim.ufu.br organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. tiagomineo@icbim.ufu.br – sequence: 10 givenname: Fernanda Maria surname: Santiago fullname: Santiago, Fernanda Maria email: fmsantiago@icbim.ufu.br organization: Institute of Biomedical Sciences, Laboratory of Immunoparasitology "Dr. Mario Endsfeldz Camargo", Federal University of Uberlândia, Av. Pará 1720, Uberlândia 38400-902, Brazil. fmsantiago@icbim.ufu.br
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Keywords	Toxoplasma gondii Odontomachus bauri crude venom proteases
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SubjectTerms	Animals Ant Venoms - enzymology Ant Venoms - toxicity Anti-Bacterial Agents - toxicity Antiparasitic Agents - toxicity Ants Cell Survival - drug effects Coagulants - toxicity crude venom Erythrocytes - drug effects Escherichia coli - drug effects Escherichia coli - genetics HeLa Cells Hemolysis Humans Insect Proteins - metabolism Macrophages - drug effects Male Mice Odontomachus bauri Peptide Hydrolases - metabolism proteases Staphylococcus aureus - drug effects Staphylococcus aureus - growth & development Toxoplasma - drug effects Toxoplasma - pathogenicity Toxoplasma gondii
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Title	Biological and Enzymatic Characterization of Proteases from Crude Venom of the Ant Odontomachus bauri
URI	https://www.ncbi.nlm.nih.gov/pubmed/26633501 https://search.proquest.com/docview/1744660556 https://pubmed.ncbi.nlm.nih.gov/PMC4690119 https://doaj.org/article/85da2cc9d4f340f295876f889465e041
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