User:Marvin O'Neal/OspC: Difference between revisions

<scene name='Studio:G4SecL04/Major_antigenic_site/1' >most antigenic sites</scene>

of OspC due to the presence of variable surface-exposed residues among OspC isolates. <ref>Earnhart C, LeBlanc D, Alix K, Desrosiers D, Radolf J, and Marconi R. 2010. Identification of residues within ligand-binding domain 1 (LBD1) of the ''Borrelia burgdorferi'' OspC protein required for function in the mammalian environment. Molecular Microbiology 76(2): 393-408. [http://dx.crossref.org/10.1111%2Fj.1365-2958.2010.07103.x DOI: 10.1111/j.1365-2958.2010.07103.x]</ref>. However, among these variable regions, the outer surface-exposed residues connecting the helices α1 and α2, forming the loops,  

<scene name='Studio:G4SecL04/L1/3' >L1</scene> (residues 74-78),  

<scene name='Studio:G4SecL04/L2/2' >L2</scene> (residues 81-87),   

<scene name='Studio:G4SecL04/L3/2' >L3</scene> (residues 90-93)and two short beta strands, β1 and β2, and also  

<scene name='Studio:G4SecL04/L5/2' >L5</scene> (residues 146-150)

<scene name='Studio:G4SecL04/L4/1' >L4</scene> (residues 115-119)and  

<scene name='Studio:G4SecL04/L6/1'>L6</scene> (residues 161-169). Consequently, the surface potential of red region that projects away from the membrane is negatively charged and mainly involved in the protein-protein or protein-ligand interactions <ref name= variable>PMID: 11139584 </ref>. Only four types of oMGs (A, B, I and K), whose surface potential in red region is highly negative relative to non-invasive one plays a major role in pathogenesis of human Lyme disease  

<scene name='Studio:G4SecL04/82/1' >His82</scene>, located on the red region at the membrane distal end is unique that the replacement of other residues except His82, Lys82, Gln82, which are present only in four invasive oMGs enhances the possibility of turning invasive strains to non-invasive one. Thus, the stronger the electrostatic potential on red region, the higher the chance for OspC to bind with positively charged host ligands. Therefore, the alternation of an amino acid residue at the 82nd position on red region not only demonstrates OspC polymorphism, but also points out the probability for turning invasive strains to non-invasive strains <ref name="human lyme disease">Kumaran D, Eswaramoorthy S, Luft B, Koide S, Dunn J, Lawson C, and Swaminathan S. 2001. Crystal Structure of Outer Surface Protein C (OspC) from the Lyme Disease Spirochete, ''Borrelia burgdorferi''. The EMBO Journal 20(5): 971-978. [http://dx.crossref.org/10.1093%2Femboj%2F20.5.971 DOI:  10.1093/emboj/20.5.971]</ref>.