OspA L03 Group2: Difference between revisions

Borrelia bacteria differntially immunogenic express outer surface proteins (Wagner, 2012). One outersurface protein, OspA is a lipoprotein that was found to inhibit bacterial transmission <ref name=Ding >PMID: 11183781</ref>. OspA known as a potent stimulator of neutrophils was able to kill the pathogen and attract leukocytes. The interaction of OspA on the antigen and the antibodies was a cascade complement system. Once the complement found OspA on borrelia, it induced an innate response of [http://en.wikipedia.org/wiki/Phagocytosis phagocytosis] allowing the release of proinflammatory cytokines in a host <ref name=Ruprecht >PMID: 18097481</ref> and avoid contracting Lyme disease as it affects the heart, joints, and central nervous system <ref name=Ruprecht >PMID: 18097481</ref>.

Once entered the host through the skin or blood stream, Borrelia burgdorferi downregulated and suppressed OspA to minimize all of the host’s immunogenic characteristics <ref name=Ruprecht >PMID: 18097481</ref>, while expression of OspC was active. Usually, the initial stages of Lyme disease diagnosed individuals with peaked elevations of OspC up until 7-11 weeks, then later declined (Wagner, 2012). When OspA on the spirochete migrated to an inflammatory environment, it induced apoptosis on the bacteria through the activation of B-cells <ref name=Ruprecht >PMID: 18097481</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 exposing the  C-terminal to express the interaction with the Fab antigen combing site exposing the 3-loops and 49 residues involved where LA-2 makes direct contact <ref name=Ding >PMID: 11183781</ref>. Studies were shown through findings from nuclear magnetic resonance, or [http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance  NMR] and [http://en.wikipedia.org/wiki/Protein_crystallization crystallization] <ref name=Ding >PMID: 11183781</ref>.