OspA L03 Group2: Difference between revisions

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The model presented by the Protein Data Bank is OspA containing two light chains or Hybridoma Antibody LA2 (chains A and C), two heavy chains or Hyrbridoma Antibody LA2 (chains B and D), and two outer surface protein A (chains E and F).

The model presented by the Protein Data Bank is OspA containing two light chains or Hybridoma Antibody LA2 (chains A and C), two heavy chains or Hyrbridoma Antibody LA2 (chains B and D), and two outer surface protein A (chains E and F). In addition, the original PDB image suggests that the C-terminal domain was unchanged by the LA-2 binding, other than minor shifts in the conformations of all 3-loops to accommodate interactions with the Fab <ref name=Ding >PMID: 11183781</ref>.

The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding <ref name=Ding >PMID: 11183781</ref> towards developing vaccinations. The protein, OspA obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure to show the free state of the 3D model ~~exposed~~ the C-terminal.

The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding <ref name=Ding >PMID: 11183781</ref> towards developing vaccinations. The protein, OspA obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure to show the free state of the 3D model exposing the C-terminal to express the interaction with the Fab antigen combing site exposing the 3-loops where LA-2 makes direct contact <ref name=Ding >PMID: 11183781</ref>.

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 from “loop 1” 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.Residues 203 to 220 in “loop1” were represented by pale green, residues 224 to 233 in “loop 2” were colored purple and residues 246 to 257 in “loop 3” 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_208/1'>Ala208</scene> as red and <scene name='OspA_L03_Group2/Ala_215/1'>Ala215</scene> as blue 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 from “loop 1” 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.Residues 203 to 220 in “loop1” were represented by pale green, residues 224 to 233 in “loop 2” were colored purple and residues 246 to 257 in “loop 3” 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_208/1'>Ala208</scene> as red and <scene name='OspA_L03_Group2/Ala_215/1'>Ala215</scene> as blue 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>.

=='''Vaccination (La-2)'''==

Line 31:

===''Side Effects''===

Recent studies however have shown that neurological complications may appear in patients with this vaccination. This occurs because the down regulation of ~~ospA~~ from the vaccine would not be an abundant amount to activate the immune system for defense (Marks, 2011). This may then cause a wide range of adverse events such as headaches and acute neuroborreliosis(Marks, 2011).

Recent studies however have shown that neurological complications may appear in patients with this vaccination. This occurs because the down regulation of OspA from the vaccine would not be an abundant amount to activate the immune system for defense (Marks, 2011). This may then cause a wide range of adverse events such as headaches and acute neuroborreliosis(Marks, 2011).

=='''Comparing OspA , OspB , OspC'''==

OspA L03 Group2: Difference between revisions

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@@ Line 18: / Line 18: @@
 <Structure load='1FJ1'size='400'align='right'caption='Structure of OspA(PDB entry[[1FJ1]])'scene="/>
-The model presented by the Protein Data Bank is OspA containing two light chains or Hybridoma Antibody LA2 (chains A and C), two heavy chains or Hyrbridoma Antibody LA2 (chains B and D), and two outer surface protein A (chains E and F).
+The model presented by the Protein Data Bank is OspA containing two light chains or Hybridoma Antibody LA2 (chains A and C), two heavy chains or Hyrbridoma Antibody LA2 (chains B and D), and two outer surface protein A (chains E and F). In addition, the original PDB image suggests that the C-terminal domain was unchanged by the LA-2 binding, other than minor shifts in the conformations of all 3-loops to accommodate interactions with the Fab <ref name=Ding >PMID: 11183781</ref>.
-The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding <ref name=Ding >PMID: 11183781</ref> towards developing vaccinations. The protein, OspA obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure to show the free state of the 3D model exposed the C-terminal.
+The reactive LA-2 antibody was found to serve as an important epitope of Osp-A binding <ref name=Ding >PMID: 11183781</ref> towards developing vaccinations. The protein, OspA obtained from PDB was dissected to isolate and concentrate the F chain from the molecule of OspA from the crystallized structure to show the free state of the 3D model exposing the  C-terminal to express the interaction with the Fab antigen combing site exposing the 3-loops where LA-2 makes direct contact <ref name=Ding >PMID: 11183781</ref>.
-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 from “loop 1” 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.Residues 203 to 220 in “loop1” were represented by pale green, residues 224 to 233 in “loop 2” were colored purple and residues 246 to 257 in “loop 3” 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_208/1'>Ala208</scene> as red and <scene name='OspA_L03_Group2/Ala_215/1'>Ala215</scene> as blue 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 from “loop 1” 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.Residues 203 to 220 in “loop1” were represented by pale green, residues 224 to 233 in “loop 2” were colored purple and residues 246 to 257 in “loop 3” 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_208/1'>Ala208</scene> as red and <scene name='OspA_L03_Group2/Ala_215/1'>Ala215</scene> as blue 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>.
 =='''Vaccination (La-2)'''==
@@ Line 31: / Line 31: @@
 ===''Side Effects''===
-Recent studies however have shown that neurological complications may appear in patients with this vaccination. This occurs because the down regulation of ospA from the vaccine would not be an abundant amount to activate the immune system for defense (Marks, 2011). This may then cause a wide range of adverse events such as headaches and acute neuroborreliosis(Marks, 2011).
+Recent studies however have shown that neurological complications may appear in patients with this vaccination. This occurs because the down regulation of OspA from the vaccine would not be an abundant amount to activate the immune system for defense (Marks, 2011). This may then cause a wide range of adverse events such as headaches and acute neuroborreliosis(Marks, 2011).
 =='''Comparing OspA , OspB , OspC'''==