OspA L03 Group2: Difference between revisions
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The following is the fit mechanism where the conformations recognize LA-2 and shifts to optimize the complementary antigen combing site (Ding, 2000). There were 49 residues from the “three loops” involved that significantly affected by LA-2 binding, through findings from NMR and crystallization <ref name=Ding >PMID: 11183781</ref>. Residues 207 and 227 were excluded from analysis because of the peak overlap <ref name=Ding >PMID: 11183781</ref>. The portion of the protein chain detected through 15N-HSQC NMR that were affected by the binding of LA2 <ref name=Ding >PMID: 11183781</ref> was highlighted.<scene name='OspA_L03_Group2/Residues_203-220_loop1/2'>Residues 203 to 220 in "loop 1"</scene>” were represented by pale green, <scene name='OspA_L03_Group2/Residues_224-233_loop2/2'>residues 224-233 in loop 2</scene> were colored purple and <scene name='OspA_L03_Group2/Residues_246-257_loop3/3'>residues 247-257 in "loop 3"</scene>” were colored medium slate blue. The cool coloring of the residues shows the location of LA-2’s direct contact on the “3 loops”. Primary colors were used to represent <scene name='OspA_L03_Group2/Ala_208/4'>Ala-208</scene> as orange and <scene name='OspA_L03_Group2/Ala_215/4'>Ala-215</scene> as yellow in spacefills for the primary or initial identification of the LA-2 epitope on the beta-strands. The coloration of resides are all at one end, C-terminal of the isolated OspA molecule showing the side where LA-2 binds. The rest of the model were beta-sheets that were left yellow, as the neutral color, and the only alpha-helix was colored pink, to show the general overall structure of 21 anti-parrallel beta-strands to 1 alpha-helix <ref name=Ding >PMID: 11183781</ref>. | The following is the fit mechanism where the conformations recognize LA-2 and shifts to optimize the complementary antigen combing site (Ding, 2000). There were 49 residues from the “three loops” involved that significantly affected by LA-2 binding, through findings from NMR and crystallization <ref name=Ding >PMID: 11183781</ref>. Residues 207 and 227 were excluded from analysis because of the peak overlap <ref name=Ding >PMID: 11183781</ref>. The portion of the protein chain detected through 15N-HSQC NMR that were affected by the binding of LA2 <ref name=Ding >PMID: 11183781</ref> was highlighted.<scene name='OspA_L03_Group2/Residues_203-220_loop1/2'>Residues 203 to 220 in "loop 1"</scene>” were represented by pale green, <scene name='OspA_L03_Group2/Residues_224-233_loop2/2'>residues 224-233 in loop 2</scene> were colored purple and <scene name='OspA_L03_Group2/Residues_246-257_loop3/3'>residues 247-257 in "loop 3"</scene>” were colored medium slate blue. The cool coloring of the residues shows the location of LA-2’s direct contact on the “3 loops”. Primary colors were used to represent <scene name='OspA_L03_Group2/Ala_208/4'>Ala-208</scene> as orange and <scene name='OspA_L03_Group2/Ala_215/4'>Ala-215</scene> as yellow in spacefills for the primary or initial identification of the LA-2 epitope on the beta-strands. The coloration of resides are all at one end, C-terminal of the isolated OspA molecule showing the side where LA-2 binds. The rest of the model were beta-sheets that were left yellow, as the neutral color, and the only alpha-helix was colored pink, to show the general overall structure of 21 anti-parrallel beta-strands to 1 alpha-helix <ref name=Ding >PMID: 11183781</ref>. | ||
=='''Vaccinations | =='''Vaccinations'''== | ||
OspA is the least variable protein located on the outer surface of the borrelia bacteria <ref name=Ding >PMID: 11183781</ref>. This results in fewer mutations to occur allowing the same [http://en.wikipedia.org/wiki/Vaccine vaccine] to stay in use for a longer time. Individuals who were bit by an infected tick and received the ospA vaccine were able to produce anti-opsA antibodies. These antibodies enter the tick through its blood meal into the gut where spirochetes are found and are destroyed by the antibody’s detection of opsA. Therefore, before the spirochete enters the host, it will be inactivated and Lyme Disease may be prevented (Marks, 2011). | OspA is the least variable protein located on the outer surface of the borrelia bacteria <ref name=Ding >PMID: 11183781</ref>. This results in fewer mutations to occur allowing the same [http://en.wikipedia.org/wiki/Vaccine vaccine] to stay in use for a longer time. Individuals who were bit by an infected tick and received the ospA vaccine were able to produce anti-opsA antibodies. These antibodies enter the tick through its blood meal into the gut where spirochetes are found and are destroyed by the antibody’s detection of opsA. Therefore, before the spirochete enters the host, it will be inactivated and Lyme Disease may be prevented (Marks, 2011). | ||