StudioG24SecL04Tpc5: Difference between revisions

The outer surface lipoprotein of ''Borrelia burgdorferi'' [http://en.wikipedia.org/wiki/Borrelia_burgdorferi] uses antigenic variation via gene conversion to evade host immune response. Crystal structure of VlsE1, a recombinant variant protein of VlsE, reveals six <scene name='StudioG24SecL04Tpc5/Variable_region/2'>variable regions</scene> that form loop structures that entirely cover the membrane distal end of the protein. <ref>PMID: 11923306</ref> Almost 50% of the variable region’s surface area is exposed on the surface of  

<scene name='StudioG24SecL04Tpc5/Vlse_cassete_region_highlight/1'>VlsE</scene>. There are three major areas of the membrane distal portion on the protein surface that undergo antigenic variation [http://en.wikipedia.org/wiki/Antigenic_variation]. <ref>PMID: 11923306</ref> It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the epitopes [http://en.wikipedia.org/wiki/Epitope] throughout each variable region. Immune systems are overwhelmed with an astronomical number of different antigens. The loop structures cover predominantly the α-helical invariant regions of the protein. <ref>PMID: 11923306</ref>It is speculated that the locations of these variable regions on the membrane distal end shield the conserved regions of VlsE from antibody interaction and thereby contribute to immune evasion. <ref>PMID: 11923306</ref>