Search

Background Bovine tuberculosis and tuberculosis are chronic infectious diseases caused by the Mycobacterium tuberculosis complex members, Mycobacterium bovis and Mycobacterium tuberculosis, respectively. Infection with M. bovis and M. tuberculosis have significant implications for wildlife species management, public health, veterinary disease control, and conservation endeavours. Results Here we describe the first use of the VetMAX™ Mycobacterium tuberculosis complex (MTBC) DNA quantitative real-time polymerase chain reaction (qPCR) detection kit for African wildlife samples. DNA was extracted from tissues harvested from 48 African buffaloes and MTBC DNA was detected (test-positive) in all 26 M. bovis culture-confirmed animals with an additional 12 PCR-positive results in culture-negative buffaloes (originating from an exposed population). Of six MTBC-infected African rhinoceros tested, MTBC DNA was detected in antemortem and postmortem samples from five animals. The PCR was also able to detect MTBC DNA in samples from two African elephants confirmed to have M. bovis and M. tuberculosis infections (one each). Culture-confirmed uninfected rhinoceros and elephants’ samples tested negative in the PCR assay. Conclusions These results suggest this new detection kit is a sensitive screening test for the detection of MTBC-infected African buffaloes, African elephants and white rhinoceros.

Non conserved amino acids, which are located in the postulated α-helical region of the third zinc finger in human transcription factor SP1, have been replaced by amino acids, which occur at the analogous zinc finger position in human protein Kox 15. This helical domain was mutated from SP D HL SK H to S S HL IQ H (SP1-M3). Aspartic acid (D), serine (S) and lysine (K) were substituted by serine (S), isoleucine (I) and glutamine (Q). The DNA binding of the mutated SP1-M3 protein to the SP 1 cognate target site GGG GCG GGG was significantly impaired, indicating that the amino acids, aspartic acid, serine and lysine play a pivotal role in DNA recognition. The mutated SP1 finger cannot imitate the function of the wild type SP1 finger in interacting with the cognate SP1 target site. This structure-function analysis indicates that the third SP1 zinc finger participates in sequence-specific DNA recognition. Thus, the affinity of zinc finger domains can be altered by substituting a limited number of amino acids. This observation is consistent with the notion that zinc finger domains are positioned in the major groove of the DNA and wrap around the DNA. Structure-function analysis of this kind might lead to the description of a zinc finger specific recognition code.