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dc.provenanceComisión de Investigaciones Científicas-
dc.contributorMuñoz, Fernando F.-
dc.contributorMendieta, Julieta Renée-
dc.contributorPagano, Mariana R.-
dc.contributorPaggi, Roberto A.-
dc.contributorDaleo, Gustavo Raúl-
dc.contributorGuevara, María G.-
dc.creatorMuñoz, Fernando F.-
dc.creatorMendieta, Julieta Renée-
dc.creatorPagano, Mariana R.-
dc.creatorPaggi, Roberto A.-
dc.creatorDaleo, Gustavo Raúl-
dc.creatorGuevara, María G.-
dc.date2010-02-03-
dc.date.accessioned2019-04-29T16:07:57Z-
dc.date.available2019-04-29T16:07:57Z-
dc.date.issued2010-02-03-
dc.identifierhttp://digital.cic.gba.gob.ar/handle/11746/5367-
dc.identifierRecurso Completo-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/309977-
dc.descriptionPlant-specific insert domain (PSI) is a region of approximately 100 amino acid residues present in most plant aspartic protease (AP) precursors. PSI is not a true saposin domain; it is the exchange of the N- and C-terminal portions of the saposin like domain. Hence, PSI is called a swaposin domain. Here, we report the cloned, heterologous expression and purification of PSI from StAsp 1 (Solanum tuberosum aspartic protease 1), called StAsp-PSI. Results obtained here show that StAsp-PSI is able to kill spores of two potato pathogens in a dose-dependent manner without any deleterious effect on plant cells. As reported for StAPs (S. tuberosum aspartic proteases), the StAsp-PSI ability to kill microbial pathogens is dependent on the direct interaction of the protein with the microbial cell wall/or membrane, leading to increased permeability and lysis. Additionally, we demonstrated that, like proteins of the SAPLIP family, StAsp-PSI and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner. The amino acid residues conserved in SP_B (pulmonary surfactant protein B) and StAsp-PSI could explain the cytotoxic activity exerted by StAsp-PSI and StAPs against Gram-positive bacteria. These results and data previously reported suggest that the presence of the PSI domain in mature StAPs could be related to their antimicrobial activity-
dc.formatapplication/pdf-
dc.format7 p.-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International (BY-NC-ND 4.0)-
dc.sourcereponame:CIC Digital (CICBA)-
dc.sourceinstname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires-
dc.sourceinstacron:CICBA-
dc.source.urihttp://digital.cic.gba.gob.ar/handle/11746/5367-
dc.source.uriRecurso Completo-
dc.subjectBiología Celular, Microbiología-
dc.titleSwaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/submittedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: Comisión de Investigaciones Científicas de la Prov. de Buenos Aires

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