G14secL04Tpc3: Difference between revisions

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== Lyme Disease and OspB protein==  
== 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 [http://en.wikipedia.org/wiki/Lipoprotein 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, promoting the attachment of spirochete on the tick gut.  It’s speculated 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 [http://en.wikipedia.org/wiki/Complement_system complement], which is normally part of the immune response to bacteria. However, it remains unclear how binding of H6831 or CB2 can lead directly to lysis of the bacterium.
 
===Symptoms and Origin of Lyme disease===
 
Lyme disease is caused by the bacterial spirochete ''Borrelia burgdorferi sensu lato''. It is an inflammatory disorder that usually begins with skin lesions known as erythema chronicum migrands (ECM)<ref name ="sbu">http://www.jstor.org/stable/1689391</ref>.
Months later the skin lesion can be followed by cardiac or neurological symptoms, migratory polyarthritis, oligoarticular arthritis, and chronic arthritis in the knees<ref name="sbu" />. The disease was first recognized as a new form of inflammatory arthritis in Lyme, Conneticuit in 1975. Since then, the disease has been reported from many other parts of the United States<ref name="sbu" />. 
 
===Outer Surface Proteins===
 
Colonization and survival of ''Borrelia burgdorferi'' within ticks and mammals is facilitated, in part, by [http://en.wikipedia.org/wiki/Lipoprotein 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, promoting the attachment of spirochete on the tick gut.  It’s speculated 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 [http://en.wikipedia.org/wiki/Complement_system complement], which is normally part of the immune response to bacteria. However, it remains unclear how binding of H6831 or CB2 can lead directly to lysis of the bacterium.


===Transmission of Spirochete===  
===Transmission of Spirochete===