G15SecL05Tpc3: Difference between revisions
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==Osp-B/Antibody Bind Briefing (CB2)== | ==Osp-B/Antibody Bind Briefing (CB2)== | ||
Complement-independent antibodies have the ability to attack antigens directly in the absence of both complements or phagocytes. The exact mechanisms for these processes have not yet been clearly defined, though basic evidence shows that the attack of the complement-independent antibody creates a vesicle outgrowth that leads to an opening in the outer layer of the bacteria which leads to an osmotic lysis. (LaRocca et al, 2009). The monoclonal CB2 antibody binds to the Osp-B protein of the spirochete bacteria: its high affinity toward the ''Borrelia's'' epitope binding site eliminates the bacteria accordingly. Selective pressure has led to multiple Borrelia bacterium escaping. This occurrence is due to possible point mutations at the C-terminus end of the Osp-B lipoprotein; namely, an absence of the Lys 253 amino acid which promotes the binding affinity. The antigen variations of ''borrelia'' inhibits the binding affinity of the antibody to the epitope located on the Osp-B. | Complement-independent antibodies have the ability to attack antigens directly in the absence of both complements or phagocytes. The exact mechanisms for these processes have not yet been clearly defined, though basic evidence shows that the attack of the complement-independent antibody creates a vesicle outgrowth that leads to an opening in the outer layer of the bacteria which leads to an osmotic lysis. (LaRocca et al, 2009). The monoclonal CB2 antibody binds to the Osp-B protein of the spirochete bacteria: its high affinity toward the ''Borrelia's'' epitope binding site eliminates the bacteria accordingly. Selective pressure has led to multiple Borrelia bacterium escaping. This occurrence is due to possible point mutations at the C-terminus end of the Osp-B lipoprotein; namely, an absence of the Lys 253 amino acid which promotes the binding affinity. The antigen variations of ''borrelia'' inhibits the binding affinity of the antibody to the epitope located on the Osp-B (O'Hara et al, 2011). | ||
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*5. Sadziene A, Jonsson M, Bergström S, Bright RK, Kennedy RC, Barbour AG. "A Bactericidal Antibody to Borrelia burgdorferi is Directed Against a Variable Region of the OspB Protein". Infect Immun. 1994; 62(5): pp. 2037-45. | *5. Sadziene A, Jonsson M, Bergström S, Bright RK, Kennedy RC, Barbour AG. "A Bactericidal Antibody to Borrelia burgdorferi is Directed Against a Variable Region of the OspB Protein". Infect Immun. 1994; 62(5): pp. 2037-45. | ||
*6. Neelakanta G, Li X, Pal U, et al. "Outer Surface Protein B is Critical for Borrelia burgdorferi Adherence and Survival Within Ixodes Ticks". PLoS Pathog. 2007; 3(3): pp. 33 | *6. Neelakanta G, Li X, Pal U, et al. "Outer Surface Protein B is Critical for Borrelia burgdorferi Adherence and Survival Within Ixodes Ticks". PLoS Pathog. 2007; 3(3): pp. 33 | ||
*7. O'Hara N, LaRocca T, Spikes D, Miyazaki J, O'Neal M."Fundamentals of Scientific Inquiry in the Biological Sciences". Hayden-McNeil Publishing. Stony Brook University. 2011: pp. 97-117 | |||
