Science and Technology Production

The swaposin-like domain of potato aspartic protease(StAsp-PSI) exerts antimicrobial activity on plant and human pathogens.

Articulo

Authorship:

Fernando F. Muñoz, ; Julieta R. Mendieta, ; Mariana R.Pagano ; Roberto A. Paggi, ; Gustavo R. Daleo ; GUEVARA, MARIA GABRIELA

Date:

2010

Publishing House and Editing Place:

ELSEVIER SCIENCE INC

Magazine:

PEPTIDES, vol. 31 (pp. 777-785) ELSEVIER SCIENCE INC

Summary *

Plant specific insert domain (PSI) is an extra region, of 100 aminoacid residues approximately, present in most of plant aspartic proteases (AP) precursors. The real functions of PSI are still unclear; however, it has been associated with AP vacuolar transport and indirectly with AP pathogen plasma membrane leakage. Here we report on the cloned, heterologous expression and purification of PSI from StAsp 1 (Solanum tuberosum aspartic protease 1) clone, named as StAsp-PSI. Results obtained show that StAsp-PSI is able to kill spores of two potato pathogens but not plant cells, in a dose dependent manner. As reported for StAPs (Solanum tuberosum aspartic proteases), StAsp-PSI cytotoxic activity involves leakage of pathogen plasma membrane by a direct interaction with the spore surface. These results and the data previously reported suggest that the presence of PSI domain into the mature StAPs could be related with the StAPs antimicrobial activity. We demonstrated that, like proteins family (SAPLIPs), StAsp-PSI and StAPs are citotoxic for Gram – and Gram + bacteria in a dose dependent manner, but not for human red blood cells. The aminoacid 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 (+) bacteria and not found in others SAPLIPs. These results open a new perspective to analyze these proteins as possible candidates to develop new drugs that would be active against microbes but not against mammalian cells. Information provided by the agent in SIGEVA

Key Words

plant specific domainantimicrobial proteins and peptidesplant aspartic proteasesSaposin like proteins