G04SecL04Tpc1: Difference between revisions

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~~Another surface protein of note in the B. Burgdorferi is~~ <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>, ~~which is~~ 53% similar to OspB. ~~This~~ is due to ~~some structural similarities~~ in the ~~proteins~~. ***More contents will be done before noon.~~***~~

The Outer Surface Protein A, <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene> composed of C-terminal and N-terminal tips at each end. B-cell epitope on C-terminal of OspA is the one that binds with LA-2 Fab. Antibody LA-2 composed of two heavy chains and two light chains. There are three loops on OspA that are involved in an interaction with LA-2. Loop one is highlighted to be the most interact with LA-2 among the loops. This is because there is Alanine 208 on the loop one and this residue has a characteristic of protrude on a surface and it allows antibody to interact the most. This result is shown by observing antibody reactivity using different species of Borrelia transmit Lyme disease<ref name="Ding,W">PMID: 11183781</ref>.

Complex proteins OspB and OspA are shown to be 53% similar due to their protein structures<ref name="Li,H">PMID: 9108020</ref>. The H6831 and LA2 antibodies are also structurally similar and both are bind at C-terminal of the particular surface protein and H6831 and LA-2 epitopes are positioned opposite to the N-terminus that is end of each antigen. For both C-terminal tips, there are 3 loops that contributed for the interactions between antigen and antibody. The change in conformation of OspA after binding to the LA2 antibody is very similar to that of OspB when binding with H6831. However, among the three loops loop2 shown to have the most interaction for OspB complex while loop1 for OspA. The rational for this is due to the residues such as Lys253 is highlighted on Loop2 and Ala 208 on Loop1<ref name="Ding,W">PMID: 11183781</ref><ref name="Li,H">PMID: 9108020</ref>. Also, researchers found that buried surface area of OspA in LA-2 Fab is larger than OspB in the H6831Fab.(Becker et al. 2005).

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 <Structure load='1FJ1' size='300' frame='true' align='right' caption='OspA and LA2 bound complex' scene='G04SecL04Tpc1/Ospa/1' />
-Another surface protein of note in the B. Burgdorferi is <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>, which is 53% similar to OspB. This is due to some structural similarities in the proteins. ***More contents will be done before noon.***
+The Outer Surface Protein A, <scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene> composed of C-terminal and N-terminal tips at each end. B-cell epitope on C-terminal of OspA is the one that binds with LA-2 Fab. Antibody LA-2 composed of two heavy chains and two light chains. There are three loops on OspA that are involved in an interaction with LA-2. Loop one is highlighted to be the most interact with LA-2 among the loops. This is because there is Alanine 208 on the loop one and this residue has a characteristic of protrude on a surface and it allows antibody to interact the most. This result is shown by observing antibody reactivity using different species of Borrelia transmit Lyme disease<ref name="Ding,W">PMID: 11183781</ref>.
+Complex proteins OspB and OspA are shown to be 53% similar due to their protein structures<ref name="Li,H">PMID: 9108020</ref>. The H6831 and LA2 antibodies are also structurally similar and both are bind at C-terminal of the particular surface protein and H6831 and LA-2 epitopes are positioned opposite to the N-terminus that is end of each antigen. For both C-terminal tips, there are 3 loops that contributed for the interactions between antigen and antibody. The change in conformation of OspA after binding to the LA2 antibody is very similar to that of OspB when binding with H6831. However, among the three loops loop2 shown to have the most interaction for OspB complex while loop1 for OspA. The rational for this is due to the residues such as Lys253 is highlighted on Loop2 and Ala 208 on Loop1<ref name="Ding,W">PMID: 11183781</ref><ref name="Li,H">PMID: 9108020</ref>. Also, researchers found that buried surface area of OspA in LA-2 Fab is larger than OspB in the H6831Fab.(Becker et al. 2005).