IIB   20738
INSTITUTO DE INVESTIGACIONES BIOLOGICAS
Unidad Ejecutora - UE
artículos
Título:
Swaposin domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens
Autor/es:
MUÑOZ, F. F.; MENDIETA, J.; PAGANO, M.; PAGGI, R. A.; GUSTAVO RAUL DALEO; GUEVARA, M. G.
Revista:
Peptides
Editorial:
ACADEMIC PRESS INC ELSEVIER SCIENCE
Referencias:
Año: 2010 vol. 31 p. 777 - 785
ISSN:
0196-9781
Resumen:
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
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
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner
StAsp-PSI
and StAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent mannerStAPs are cytotoxic to Gram-negative and Gram-positive bacteria in a dose dependent manner