G04SecL04Tpc1: Difference between revisions

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==Introduction==

Spirochetes are motile, spiral shaped microorganisms. They have an inner membrane, a thin peptidoglycan layer and outer membrane and a periplasmic space. One well known characteristic of spirochetes is that they have lipoproteins that are surface-exposed on their outer membrane. (Connolly & Benach 2005). These proteins determine the ability of antigen to trigger an immune response. In Lyme Disease,''Borrelia Burgdorferi'', the lipoproteins are outer-surface proteins. Though it has many outer-surface proteins on its outer membrane, Outer Surfafce Protein B (Osp B) and outer surface protein A (OspA) are very important lipoproteins in Lyme Disease(Becker et al2005). They have similar structures and they both are bactericidal but they use different antibodies to lyse the bacteria.

Outer surface protein B (OspB) combines with a bactericidal fab H6831 in order to kill the bacteria ''B. Burgdoferi''. This antibody is directed towards the C-terminus and is complement-independent. This means unlike regular antibodies, it does not need to bind to complement protein in order to lyse the bacteria. The mechanism for this amazing anomaly has not yet been discovered. However, much research has been done on the particular aspects that may aid in the process. This includes various amino acid and aromatic residues.

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+==Introduction==
+Spirochetes are motile, spiral shaped microorganisms. They have an inner membrane, a thin peptidoglycan layer and outer membrane and a periplasmic space. One well known characteristic of spirochetes is that they have lipoproteins that are surface-exposed on their outer membrane. (Connolly & Benach 2005). These proteins determine the ability of antigen to trigger an immune response. In Lyme Disease,''Borrelia Burgdorferi'', the lipoproteins are outer-surface proteins. Though it has many outer-surface proteins on its outer membrane, Outer Surfafce Protein B (Osp B) and outer surface protein A (OspA) are very important lipoproteins in Lyme Disease(Becker et al2005). They have similar structures and they both are bactericidal but they use different antibodies to lyse the bacteria.
+Outer surface protein B (OspB) combines with a bactericidal fab H6831 in order to kill the bacteria ''B. Burgdoferi''.   This antibody is directed towards the C-terminus and is complement-independent. This means unlike regular antibodies, it does not need to bind to complement protein in order to lyse the bacteria. The mechanism for this amazing anomaly has not yet been discovered. However, much research has been done on the particular aspects that may aid in the process. This includes various amino acid and aromatic residues.
 <Structure load='1RJL' size='500' frame='true' align='right' caption='OspB and Fab complex' scene='G04SecL04Tpc1/1rjl/1' />