User:Marvin O'Neal/OspC: Difference between revisions
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At the membrane distal region, the six loop regions, including two β-strands illustrates the | At the membrane distal region, the six loop regions, including two β-strands illustrates the | ||
<scene name='Studio:G4SecL04/Most_antigenic_site/1'>most antigenic sites</scene> | <scene name='Studio:G4SecL04/Most_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> | 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 <font color='red'>variable regions</font color>, the outer surface-exposed residues connecting the helices α1 and α2, forming the loops, | ||
<scene name='Studio:G4SecL04/L1/4'>L1</scene> (residues 74-78), | <scene name='Studio:G4SecL04/L1/4'>L1</scene> (residues 74-78), | ||
<scene name='Studio:G4SecL04/L2/3'>L2</scene> (residues 81-87), | <scene name='Studio:G4SecL04/L2/3'>L2</scene> (residues 81-87), | ||
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are more highly variable than those present in the loops, | are more highly variable than those present in the loops, | ||
<scene name='Studio:G4SecL04/L4/2'>L4</scene> (residues 115-119)and | <scene name='Studio:G4SecL04/L4/2'>L4</scene> (residues 115-119)and | ||
<scene name='Studio:G4SecL04/L6/3'>L6</scene> (residues 161-169). Consequently, the surface potential of <font color='red'>red region</font color> 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> | <scene name='Studio:G4SecL04/L6/3'>L6</scene> (residues 161-169). Consequently, the surface potential of <font color='red'>red region</font color> 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 <font color='red'>red region</font color> is highly negative relative to non-invasive one plays a major role in pathogenesis of human Lyme disease. | ||
<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> | <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> | ||
The residue, | The residue, | ||
<scene name='Studio:G4SecL04/His_82/1'>His82</scene>, located on the <font color='red'>red region</font color> 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 <font color='red'>red region</font color>, 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 <font color='red'>red region</font color> 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> | <scene name='Studio:G4SecL04/His_82/1'>His82</scene>, located on the <font color='red'>red region</font color> 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 <font color='red'>red region</font color>, 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 <font color='red'>red region</font color> 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> | ||
==References== | ==References== | ||
<references /> | <references /> | ||
