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Role of AprA and pyocyanin from Pseudomonas aeruginosa on Staphylococcus aureus tolerance to silver.

The opportunistic pathogens Staphylococcus aureus and Pseudomonas aeruginosa are often found together causing persistent infections where they exhibit complex interactions that affect their virulence and resistance to treatment. We sought to clarify how interactions between these organisms affect their resistance to the antimicrobial metal silver (AgNO3). As previous work showed that cell-free supernatant from P. aeruginosa enhances the resistance of S. aureus, we aimed to identify the exact factor(s) responsible for this increase. Using molecular weight cutoff filters and proteomics, we identified the protein AprA and pyocyanin as the responsible factors. Transposon-mediated disruption of aprA led to the production of supernatant which could not enhance the silver tolerance of S. aureus. These findings suggest that the protease AprA from P. aeruginosa plays an important role in increasing the tolerance of S. aureus to AgNO3 via in part by mediating the levels of pyocyanin which in turn reduces Ag2+ to detoxify it.

Pseudomonas aeruginosa

Active and inactive renin in normal human plasma. Comparison between acid activation and cryoactivation.

Inactive renin in human plasma is converted to active renin in vitro by acid activation or by cryoactivation. Renin activity was measured at pH 5.5 and renin concentration at pH 7.4. The plasma renin activity before and after cryo-treatment is termed active (APRA) and total (TPRA) plasma renin activity; the plasma renin concentration before and after acid treatment active (APRC) and total (TPRC) plasma renin concentration. In this study we demonstrated that in normal subjects the proportion of active to total renin after cryo-treatment averaged 61%, which was significantly (p less than 0.001) higher than the mean percentage active renin of 34 found with the acid activation procedure. Plasma angiotensin II correlated significantly with APRA, TPRA, TPRC and plasma angiotensin I (PA I), but not with inactive renin, which suggests that inactive renin does not produce angiotensin II in vivo. Cold treatment after acid activation and acid treatment after cryoactivation did not provoke a significant change in the measured renin concentration. Our data support the view that acidification of the plasma activates more than does cryo-treatment, and that inactive renin does not contribute to plasma angiotensin II.

Acids