Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens
- Autores
- Muñoz, Fernando F.; Mendieta, Julieta Renée; Pagano, Mariana R.; Paggi, Roberto A.; Daleo, Gustavo Raúl; Guevara, María G.
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión enviada
- Descripción
- 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
- Materia
-
Biología Celular, Microbiología
Plant specific domain
SAPLIPs
Antimicrobial proteins - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-nd/4.0/
- Repositorio
- Institución
- Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
- OAI Identificador
- oai:digital.cic.gba.gob.ar:11746/5367
Ver los metadatos del registro completo
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Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogensMuñoz, Fernando F.Mendieta, Julieta RenéePagano, Mariana R.Paggi, Roberto A.Daleo, Gustavo RaúlGuevara, María G.Biología Celular, MicrobiologíaPlant specific domainSAPLIPsAntimicrobial proteinsPlant-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 activity2010-02-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/5367enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.peptides.2010.02.001info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-09-29T13:40:08Zoai:digital.cic.gba.gob.ar:11746/5367Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-09-29 13:40:09.028CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse |
dc.title.none.fl_str_mv |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
title |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
spellingShingle |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens Muñoz, Fernando F. Biología Celular, Microbiología Plant specific domain SAPLIPs Antimicrobial proteins |
title_short |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
title_full |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
title_fullStr |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
title_full_unstemmed |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
title_sort |
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens |
dc.creator.none.fl_str_mv |
Muñoz, Fernando F. Mendieta, Julieta Renée Pagano, Mariana R. Paggi, Roberto A. Daleo, Gustavo Raúl Guevara, María G. |
author |
Muñoz, Fernando F. |
author_facet |
Muñoz, Fernando F. Mendieta, Julieta Renée Pagano, Mariana R. Paggi, Roberto A. Daleo, Gustavo Raúl Guevara, María G. |
author_role |
author |
author2 |
Mendieta, Julieta Renée Pagano, Mariana R. Paggi, Roberto A. Daleo, Gustavo Raúl Guevara, María G. |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Biología Celular, Microbiología Plant specific domain SAPLIPs Antimicrobial proteins |
topic |
Biología Celular, Microbiología Plant specific domain SAPLIPs Antimicrobial proteins |
dc.description.none.fl_txt_mv |
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 |
description |
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 |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-02-03 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/submittedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
submittedVersion |
dc.identifier.none.fl_str_mv |
https://digital.cic.gba.gob.ar/handle/11746/5367 |
url |
https://digital.cic.gba.gob.ar/handle/11746/5367 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.peptides.2010.02.001 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-nd/4.0/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ |
dc.format.none.fl_str_mv |
application/pdf |
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CIC Digital (CICBA) |
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CIC Digital (CICBA) |
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Comisión de Investigaciones Científicas de la Provincia de Buenos Aires |
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CICBA |
institution |
CICBA |
repository.name.fl_str_mv |
CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires |
repository.mail.fl_str_mv |
marisa.degiusti@sedici.unlp.edu.ar |
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13.070432 |