G12SecL02Tpc3: Difference between revisions
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==Introduction== | ==Introduction== | ||
Borrelia burgdorferi is a gram-negative spirochete that is the causative agent of Lyme disease. It’s transmitted to humans through hard-bodied ticks of the genus Ixodes. In order for this microbe to survive and proliferate in its various environments, it possesses many different lipid anchored outer surface proteins, including OspB. | ''Borrelia burgdorferi'' is a gram-negative spirochete that is the causative agent of Lyme disease. It’s transmitted to humans through hard-bodied ticks of the genus Ixodes. In order for this microbe to survive and proliferate in its various environments, it possesses many different lipid anchored outer surface proteins, including OspB. | ||
In conjunction with OspA, OspB allows B. burgdorferi to adhere to the midgut of the tick host. Once inside the human host, the epitopes on OspB are recognized by the immune system. Certain complement independent antibodies, H6831 and CB2, are able to lyse the microbes without help from WBCs. Recognition of the OspB epitope by either antibody is dependent on the lys-253 side chain; mutations that lead to any other amino acid in that position reduces binding affinity dramatically. Studies have shown that binding to the epitope induces conformational changes in the liporotein that may lead to the lysing of the cell. | In conjunction with OspA, OspB allows B. burgdorferi to adhere to the midgut of the tick host. Once inside the human host, the epitopes on OspB are recognized by the immune system. Certain complement independent antibodies, H6831 and CB2, are able to lyse the microbes without help from WBCs. Recognition of the OspB epitope by either antibody is dependent on the lys-253 side chain; mutations that lead to any other amino acid in that position reduces binding affinity dramatically. Studies have shown that binding to the epitope induces conformational changes in the liporotein that may lead to the lysing of the cell. | ||
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Examining the global dynamics of the antigen + Fab by NMR methods have shown that the effects of binding can be propagated to regions of the antigen that are distant to the epitope, which would be critical to the auto proteolytic removal of strands 1-4. | Examining the global dynamics of the antigen + Fab by NMR methods have shown that the effects of binding can be propagated to regions of the antigen that are distant to the epitope, which would be critical to the auto proteolytic removal of strands 1-4. | ||