G12SecL02Tpc3: Difference between revisions
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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. | ||
==Structure== | ==Structure== | ||
==Functionality== | ==Functionality== | ||
===In Vector=== | ===In Vector=== | ||
===In Host=== | ===In Host=== | ||
