StudioG24SecL04Tpc5: Difference between revisions

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===Variable Region===

The outer surface lipoprotein of ''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 [http://en.wikipedia.org/wiki/Antigenic_variation antigenic variation]<br>.<ref>PMID: 11923306</ref> It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the [http://en.wikipedia.org/wiki/Epitope epitope]<br>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>

<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 [http://en.wikipedia.org/wiki/Antigenic_variation antigenic variation.]<br><ref>PMID: 11923306</ref>It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the [http://en.wikipedia.org/wiki/Epitope epitope]<br>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>

In the experimental infection of mice, segments of the silent cassette recombines via gene conversion mechanism into the ''vlsE'' cassette region. The changes in sequence were detected after 4 days after experimental infection in mice. 28 days later, every skin isolate and other tissues were unique in that they contained about 9-13 recombination events. It is hypothesized that the humoral immune response cannot cope to a seemingly continuous generation of VlsE variants. This permits immune evasion and persistent infection.<ref>PMID: 11923306</ref>

===Invariable===

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@@ Line 23: / Line 23: @@
 ===Variable Region===
 The outer surface lipoprotein of ''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 [http://en.wikipedia.org/wiki/Antigenic_variation antigenic variation]<br>.<ref>PMID: 11923306</ref> It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the [http://en.wikipedia.org/wiki/Epitope epitope]<br>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>
+<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 [http://en.wikipedia.org/wiki/Antigenic_variation antigenic variation.]<br><ref>PMID: 11923306</ref>It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the [http://en.wikipedia.org/wiki/Epitope epitope]<br>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>
+In the experimental infection of mice, segments of the silent cassette recombines via gene conversion mechanism into the ''vlsE'' cassette region. The changes in sequence were detected after 4 days after experimental infection in mice. 28 days later, every skin isolate and other tissues were unique in that they contained about 9-13 recombination events. It is hypothesized that the humoral immune response cannot cope to a seemingly continuous generation of VlsE variants. This permits immune evasion and persistent infection.<ref>PMID: 11923306</ref>
 ===Invariable===