AI Article Synopsis
- Researchers isolated and purified a caseinolytic protease from Nocardia brasiliensis, using techniques like polyacrylamide gel electrophoresis for this purpose.
- When injected into mice, the purified protease triggered the production of IgM and IgG antibodies and effectively prevented mycetoma development in infected animals through active immunization.
- Despite having a high concentration of anti-protease antibodies, hyperimmune sera collected 60 days post-immunization lost its protective effects, suggesting that cytokines may play a role in this phenomenon.
Article Abstract
We isolated and purified to homogeneity a caseinolytic protease from a Nocardia brasiliensis cell extract. Preparative polyacrylamide gel electrophoresis and electroelution were employed for purification. This purified protease was injected in BALB/c mice and induced IgM and IgG anti-protease antibodies. Active immunization of mice with this protease prevented mycetoma development in experimentally infected animals. Passive immunization with hyperimmune sera containing a high anti-protease antibody titer conferred partial but transient protection when collected 30 days after donor's immunization. The protective effect of hyperimmune sera was lost when obtained from donors after 60 days from their immunization despite its higher anti-protease antibody concentration. Cytokines are good candidates to explain these findings.
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| http://dx.doi.org/10.1016/S0928-8244(03)00102-0 | DOI Listing |
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