G15SecL05Tpc3: Difference between revisions

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Crytsallization, binding and X-ray diffraction analysis of Osp-B along with a sampling of its complement-independent antibodies have shown that its structure is analogous to that of Osp-A, with a significant difference: within each borrelia species, Osp-A is largely invariant in amino acid sequence and antigenic reactivity, but Osp-B varies significantly (Becker et al, 2005). These variations inhibit the ability of scientists to develop Osp-B as a protective vaccine against Lyme borreliosis. Osp-B’s variations are primarily expressed as significant differences of reactivity with monoclonal antibodies and truncation of the C-terminus; this proves problematic for vaccine development since most protective antibodies targeted against Osp-A and Osp-B are generally directed toward this terminus region. Variations such as truncation in Osp-B can inhibit this process making the vaccine ineffective, though certain complement independent antibodies such as the samples examined in the crystallization process have been found to bind and lyse Osp-B in the absence of complement.