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Immunological cross-reactivity of mycobacterial topoisomerase I and divergence from other bacteria

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
Publication: Tuberculosis
Publisher: Elsevier Science
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
URI: http://eprints.iisc.ac.in/id/eprint/22618

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