G14secL04Tpc3: Difference between revisions

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== Lyme Disease and OspB protein==

Lyme disease is caused by the bacterial spirochete Borrelia burgdorferi sensu lato. Colonization and survival of Borrelia burgdorferi within ticks and mammals is facilitated, in part, by lipoproteins. OspB and OspA are two of the major lipoproteins present on the outer surface of the spirochete Borrelia Burgdoferi. Studies have shown that OspB is critical for the adherence of the spirochete to the gut wall of its tick vector. The free OspB structure consists of a barrel domain which might be the portion that interacts with a protein or a linear saccharide in the tick-gut (17368), promoting the attachment of spirochete on the tick gut. It’s believed that destroying these lipoproteins will cause bacterial death of spirochetes. Some antibody Fab fragments such as H6831 and CB2 have been shown to cause bacterial lysis of spirochetes by binding to these lipoproteins in the absence of phagocytes and without complement, which is normally part of the immune response to bacteria. However, it is unclear how binding of H6831 or CB2 can lead directly to lysis of the bacterium.

[Lyme disease] is caused by the bacterial spirochete Borrelia burgdorferi sensu lato. Colonization and survival of Borrelia burgdorferi within ticks and mammals is facilitated, in part, by lipoproteins. OspB and OspA are two of the major lipoproteins present on the outer surface of the spirochete Borrelia Burgdoferi. Studies have shown that OspB is critical for the adherence of the spirochete to the gut wall of its tick vector. The free OspB structure consists of a barrel domain which might be the portion that interacts with a protein or a linear saccharide in the tick-gut (17368), promoting the attachment of spirochete on the tick gut. It’s believed that destroying these lipoproteins will cause bacterial death of spirochetes. Some antibody Fab fragments such as H6831 and CB2 have been shown to cause bacterial lysis of spirochetes by binding to these lipoproteins in the absence of phagocytes and without complement, which is normally part of the immune response to bacteria. However, it is unclear how binding of H6831 or CB2 can lead directly to lysis of the bacterium.

==Free OspB structure==

G14secL04Tpc3: Difference between revisions

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 == Lyme Disease and OspB protein==
-Lyme disease is caused by the bacterial spirochete Borrelia burgdorferi sensu lato. Colonization and survival of Borrelia burgdorferi within ticks and mammals is facilitated, in part, by lipoproteins. OspB and OspA are two of the major lipoproteins present on the outer surface of the spirochete Borrelia Burgdoferi. Studies have shown that OspB is critical for the adherence of the spirochete to the gut wall of its tick vector. The free OspB structure consists of a barrel domain which might be the portion that interacts with a protein or a linear saccharide in the tick-gut (17368), promoting the attachment of spirochete on the tick gut.  It’s believed that destroying these lipoproteins will cause bacterial death of spirochetes.  Some antibody Fab fragments such as H6831 and CB2 have been shown to cause bacterial lysis of spirochetes by binding to these lipoproteins in the absence of phagocytes and without complement, which is normally part of the immune response to bacteria. However, it is unclear how binding of H6831 or CB2 can lead directly to lysis of the bacterium.
+[Lyme disease] is caused by the bacterial spirochete Borrelia burgdorferi sensu lato. Colonization and survival of Borrelia burgdorferi within ticks and mammals is facilitated, in part, by lipoproteins. OspB and OspA are two of the major lipoproteins present on the outer surface of the spirochete Borrelia Burgdoferi. Studies have shown that OspB is critical for the adherence of the spirochete to the gut wall of its tick vector. The free OspB structure consists of a barrel domain which might be the portion that interacts with a protein or a linear saccharide in the tick-gut (17368), promoting the attachment of spirochete on the tick gut.  It’s believed that destroying these lipoproteins will cause bacterial death of spirochetes.  Some antibody Fab fragments such as H6831 and CB2 have been shown to cause bacterial lysis of spirochetes by binding to these lipoproteins in the absence of phagocytes and without complement, which is normally part of the immune response to bacteria. However, it is unclear how binding of H6831 or CB2 can lead directly to lysis of the bacterium.
 ==Free OspB structure==