G13secL03Tpc3: Difference between revisions

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==Application==

OspB is capable of existing in various forms~~, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody~~. ~~<ref name=Article4> PMID: 15128807 </ref>~~ Mutations occur in the residue of Lysine, ~~which~~ prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines ~~for Osp B~~ have not yet been ~~discovered~~ due to the increased variability in the ~~epitope, as the vaccine wouldn’t be~~ able to counteract ~~a wide variety of~~ strains of ~~“Borrelia~~.” However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research as it is still currently misunderstood.

Under pressure in the presence of antibodies, OspB is capable of existing in various forms. Mutations occur in the residue of Lysine 253, the epitope of H6831, and may prevent Borrelia from being recognized and lysed by bactericidal Fabs such as H6381. <ref name=Article4> PMID: 15128807 </ref> The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines created to specifically fight OspB have not yet been successful, due to the increased variability of the epitop. Vaccine are not yet able to counteract the varied strains of Borrelia burgdorferi. However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research, as it is still currently misunderstood.

References: {{reflist}}

G13secL03Tpc3: Difference between revisions

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@@ Line 23: / Line 23: @@
 ==Application==
-OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. <ref name=Article4> PMID: 15128807 </ref>  Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines for Osp B have not yet been discovered due to the increased variability in the epitope, as the vaccine wouldn’t be able to counteract a wide variety of strains of “Borrelia.” However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research as it is still currently misunderstood.
+Under pressure in the presence of antibodies, OspB is capable of existing in various forms. Mutations occur in the residue of Lysine 253, the epitope of H6831, and may prevent Borrelia from being recognized and lysed by bactericidal Fabs such as H6381. <ref name=Article4> PMID: 15128807 </ref> The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines created to specifically fight OspB have not yet been successful, due to the increased variability of the epitop. Vaccine are not yet able to counteract the varied strains of Borrelia burgdorferi. However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research, as it is still currently misunderstood.
 References: {{reflist}}