Bacillus anthracis is the anthrax-causing organism prevalent in livestock and every so often found in human beings. B anthracis emits toxins that majorly subdue the host’s defence mechanism while producing effector proteins whose role is yet to be ascertained. The anthrax toxin is composed of three protein compositions, one of them being the suppressor-of-variegation, enhancer-of-zeste, trithorax protein commonly referred to as Ba SET. BaSET methylates the human histone H1, causing the subduing of the NF-Kb (nuclear factor kappa-light-chain-enhancer of activated B cells) functions, whose primary function is to control DNA transcription and cell survival.
The purpose of this study was to establish the role of SET protein, Ba SET, in the life cycle of B anthracis. However, it is yet to be ascertained what role Ba SET plays in the cycle of B.athracis. Functions of Ba SET were identified to distinguish its role in intensifying B.antracis’ survival in the infected host. It was also established that Ba SET is a key determinant in the subjugation of host transcription and also in the development of B.antracis.
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Certain experimental procedures were carried out, and several results were acquired. It was established that though prevalent in mammals, the distribution of SET protein modules is constrained when it comes to plants and human pathogens, inclusive of bacteria and tropical parasites. Another experiment carried out was to authenticate the potentiality of Ba SET to regulate transcription. From the findings it was safe to say that there was a high possibility that the Ba SET protein was a likely transcriptional repressor, impelling the deliberation that B.anthracis could be using Ba SET to subdue NF-Kb transcriptional activator. Another finding instigated that, the secretion of B.antracis by the SET protein is pinpointed in the nucleus of the infected bodies where methylization of the Histone H1 takes place. Nevertheless, the question raised is if the secretion of Ba SET can be discovered in the nucleus of the infected macrophages. To answer this, extracts, both cytosolic and nuclear were obtained from a macrophage cell line and infected for 2 and 4 hours respectively with B.anthracis .Adopting histone H3, as both a cytosolic marker and a nuclear, data gathered show that Ba SET is located inside the nucleus of cells. In another experiment, to ascertain whether macrophage chromatin is methylated by the Ba SET protein, nuclear extracts from infected and uninfected cells were assembled and studied at 2 and 4 hours after infection.The presence of a heavy chain comprising of Histone H1 and a polyclonal antibody was important for the experiment to breed maximum results. Data collected indicated that existence of Ba SET protein propagated to elevated levels of H1, implying that Ba SET promotes transcriptional inhibition by reconstructing chromatin modification.
The research and study has been conclusive in establishing the toxin that is the B.anthricis and further carrying out an array of experiments to support the findings. Results indicated that it is the first instance that pathogenic bacteria have used histone methylation in a bid to survive in its host.
In conclusion, the above findings have paved the way for further studies to be conducted to establish what mechanisms Ba SET uses to leave the B.athricis and enter the nucleus. Utilization of Ba SET to anatomize what role H1 plays in gene regulation. Though this is a first instance, it is likely that an existence of SET-like proteins in other pathogens may produce similar findings.
