Leelaram, Majety Naga and Bhat, Anuradha Gopal and Suneetha, Nunna and Nagaraja, Valakunja and Manjunath, Ramanathapuram (2009) Immunological cross-reactivity of mycobacterial topoisomerase I and divergence from other bacteria. In: Tuberculosis, 89 (4). pp. 256-262.
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Mycobacterium smegmatis topoisomerase I exhibits several distinctive characteristics among all topoisomerases. The enzyme is devoid of Zn2+fingers found typically in other bacterial type I topoisomerases and binds DNA in a site-specific manner. Using polyclonal antibodies, we demonstrate the high degree of relatedness of the enzyme across mycobacteria but not other bacteria. This absence of cross-reactivity from other bacteria indicates that mycobacterial topoisomerase I has diverged from Escherichia coli and other bacteria. We have investigated further the immunological properties of the enzyme by raising a panel of monoclonal antibodies that recognises different antigenically active regions of the enzyme and binds it with widely varied affinity. Inhibition of a C-terminal domain-specific antibody binding by enzyme-specific and non-specific oligonucleotides suggests the possibility of using these monoclonal antibodies to probe the structure, function and in vivo role of the enzyme.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Keywords:||Topoisomerase I;Mycobacteria;Monoclonal antibody;Relative affinity.|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||28 Aug 2009 12:26|
|Last Modified:||19 Sep 2010 05:42|
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