User:Marvin O'Neal/OspC: Difference between revisions
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/* Dilution Effect Model <ref> Ostfeld R and Keesing F. 2001. Biodiversity and Disease Risk: the Case of Lyme Disease. Conservation Biology 14.3 (2000): 722-728.[http://dx.doi.org/10.1046/j.1523-1739.2000.99014.x DOI: 10.1046/j.1523-1739.2000.99014.x |
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<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 /> | ||
