G15SecL05Tpc3: Difference between revisions

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<scene name='G15SecL05Tpc3/Not_ours/1'>ExampleNotOurs</scene>

Complement-independent antibodies have the ability to attack antigens directly in the ~~absece~~ 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 due 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'' ~~inhibit~~ 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.

==Osp-B and H6831==

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@@ Line 14: / Line 14: @@
 <scene name='G15SecL05Tpc3/Not_ours/1'>ExampleNotOurs</scene>
-Complement-independent antibodies have the ability to attack antigens directly in the absece 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 due 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'' inhibit 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.
 ==Osp-B and H6831==