antibody response to a sterile filtered ppd tuberculin in m. bovis infected and m. bovis sensitized cattle抗体反应无菌过滤产后抑郁症结核菌素在牛分枝杆菌感染牛分枝杆菌敏感的牛.pdfVIP

antibody response to a sterile filtered ppd tuberculin in m. bovis infected and m. bovis sensitized cattle抗体反应无菌过滤产后抑郁症结核菌素在牛分枝杆菌感染牛分枝杆菌敏感的牛.pdf

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antibody response to a sterile filtered ppd tuberculin in m. bovis infected and m. bovis sensitized cattle抗体反应无菌过滤产后抑郁症结核菌素在牛分枝杆菌感染牛分枝杆菌敏感的牛

Rennie et al. BMC Veterinary Research 2010, 6:50 /1746-6148/6/50 RESEARCH ARTICLE Open Access Antibody response to a sterile filtered PPD tuberculin in M. bovis infected and M. bovis sensitized cattle Bryan Rennie1,2*, Lionel G Filion2*, Nonie Smart1 Abstract 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

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