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Background  Bovine tuberculosis, caused by  Mycobacterium bovis , afflicts approximately 50 million cattle worldwide and is detected by the tuberculin skin test (TST). While it has long been recognized that purified protein derivative (PPD) tuberculin is composed of a mixture of  M. bovis  derived protein components, little is known about the quality, relative quantity and identity of the proteins that make up PPD tuberculin. We manufactured a sterile filtered PPD tuberculin (SF-PPD) from a nine-week-old  M. bovis  culture supernatant in order to characterise the culture filtrate proteins (CFP) which make up  M. bovis  PPD tuberculin and to compare the antibody response of  M. bovis  infected versus  M. bovis  sensitized cattle.    Results  SF-PPD resolved into approximately 200 discrete spots using two-dimensional polyacrylamide gel electrophoresis (2-DE) while fewer than 65 spots could be discerned from 2-DE gels of tuberculin derived from autoclaved culture supernatant. Two dimensional Western blot analyses indicated that sera from  M. bovis  sensitized cattle recognized additional SF-PPD antigens as compared to  M. bovis  infected cattle at seven weeks post infection/sensitization. However, application of a comparative tuberculin skin test resulted in an antibody boosting response to the same set of  M. bovis  CFPs in both the  M. bovis  infected and  M. bovis  sensitized cattle.    Conclusions  We concluded that it is the heat sterilization of the  M. bovis  CFPs that causes severe structural changes to the  M. bovis  proteins. This work suggests that  M. bovis  infected cattle and cattle artificially sensitized to  M. bovis  with an injection of heat killed cells exhibit similar antibody responses to  M. bovis  antigens.

Antibody response to a sterile filtered PPD tuberculin in M. bovis infected and M. bovis sensitized cattle