Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens
| cic.isFulltext | true | es |
| cic.isPeerReviewed | true | es |
| cic.lugarDesarrollo | Instituto de Investigaciones Biológicas | es |
| cic.version | info:eu-repo/semantics/submittedVersion | es |
| dc.date.accessioned | 2017-03-17T13:55:10Z | |
| dc.date.available | 2017-03-17T13:55:10Z | |
| dc.identifier.uri | https://digital.cic.gba.gob.ar/handle/11746/5367 | |
| dc.title | Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens | en |
| dc.type | Artículo | es |
| dcterms.abstract | Plant-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 | en |
| dcterms.creator.author | Muñoz, Fernando F. | es |
| dcterms.creator.author | Mendieta, Julieta Renée | es |
| dcterms.creator.author | Pagano, Mariana R. | es |
| dcterms.creator.author | Paggi, Roberto A. | es |
| dcterms.creator.author | Daleo, Gustavo Raúl | es |
| dcterms.creator.author | Guevara, María G. | es |
| dcterms.extent | 7 p. | es |
| dcterms.identifier.other | http://dx.doi.org/10.1016/j.peptides.2010.02.001 | es |
| dcterms.identifier.url | Recurso Completo | es |
| dcterms.isPartOf.issue | vol. 31 | es |
| dcterms.isPartOf.series | Peptides | es |
| dcterms.issued | 2010-02-03 | |
| dcterms.language | Inglés | es |
| dcterms.license | Attribution-NonCommercial-NoDerivatives 4.0 International (BY-NC-ND 4.0) | es |
| dcterms.subject | Plant specific domain | en |
| dcterms.subject | SAPLIPs | en |
| dcterms.subject | Antimicrobial proteins | en |
| dcterms.subject.materia | Biología Celular, Microbiología | es |
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