G13secL03Tpc3: Difference between revisions

Line 22:

==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. 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.

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.

References: {{reflist}}

G13secL03Tpc3: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 22: / Line 22: @@
 ==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. 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.
+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.
 References: {{reflist}}