G04SecL04Tpc1: Difference between revisions

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~~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 <ref name="Becker M">PMID:15713683</ref>.

Another surface protein of note in the B. Burgdorferi is outer surface protein A<scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>. It is composed of 21 anti-parallel beta-sheets and one alpha-helix. It contains a B-cell epitope on its C-terminal that binds with monoclonal antibody LA-2. LA-2 is a regular-structured antibody that is composed of two heavy chains and two light chains. <ref name="Ding,W">PMID: 11183781</ref>.

Complex proteins OspB and OspA are shown to be 53% similar due to structural similarities<ref name="Li,H">PMID: 9108020</ref>. The H6831 and LA-2 antibodies are also structurally similar, and each binds near the C-terminus on its respective surface protein. The H6831 and LA-2 epitopes on OspB and OspA are positioned at the opposite end of the molecule as the N-terminus of each antigen. On the C-terminal tips on each protein, the epitopes contain three exposed loops of residues that are involved with the binding interaction between antigen and antibody. For OspB, the middle loop (loop 2) has been shown to have the strongest interaction with H6831. The residue Lys253 in this loop is especially important in the interaction. For OspA, one of the outer loops (loop 1) has the strongest interaction with LA-2. The <scene name='G04SecL04Tpc1/Ospa_complex/6'>Alanine 208</scene> residue in the loop plays the important role here. The importance of these residues are confirmed by observing antibody reactivity using different species of Borrelia<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<ref name="Becker M">PMID:15713683</ref>).

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 <Structure load='1FJ1' size='300' frame='true' align='right' caption='OspA and LA2 bound complex' scene='G04SecL04Tpc1/Ospa/1' />
-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 <ref name="Becker M">PMID:15713683</ref>.
+Another surface protein of note in the B. Burgdorferi is outer surface protein A<scene name='G04SecL04Tpc1/Ospa_complex/1'>OspA</scene>. It is composed of 21 anti-parallel beta-sheets and one alpha-helix.  It contains a B-cell epitope on its C-terminal that binds with monoclonal antibody LA-2.  LA-2 is a regular-structured antibody that is composed of two heavy chains and two light chains. <ref name="Ding,W">PMID: 11183781</ref>.
+Complex proteins OspB and OspA are shown to be 53% similar due to structural similarities<ref name="Li,H">PMID: 9108020</ref>.  The H6831 and LA-2 antibodies are also structurally similar, and each binds near the C-terminus on its respective surface protein.  The H6831 and LA-2 epitopes on OspB and OspA are positioned at the opposite end of the molecule as the N-terminus of each antigen.  On the C-terminal tips on each protein, the epitopes contain three exposed loops of residues that are involved with the binding interaction between antigen and antibody.  For OspB, the middle loop (loop 2) has been shown to have the strongest interaction with H6831. The residue Lys253 in this loop is especially important in the interaction.  For OspA, one of the outer loops (loop 1) has the strongest interaction with LA-2. The <scene name='G04SecL04Tpc1/Ospa_complex/6'>Alanine 208</scene> residue in the loop plays the important role here.  The importance of these residues are confirmed by observing antibody reactivity using different species of Borrelia<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<ref name="Becker M">PMID:15713683</ref>).