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. Almost 50% of the variable region’s surface area is exposed on the surface of VlsE. There are three major areas of the membrane distal portion on the protein surface that undergo antigenic variation. It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the epitopes 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. 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.

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. Almost 50% of the variable region’s surface area is exposed on the surface of VlsE. 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]. 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. 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.

===Invariable===

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. Almost 50% of the variable region’s surface area is exposed on the surface of VlsE. There are three major areas of the membrane distal portion on the protein surface that undergo antigenic variation. It is likely that amino acid mutations of these residues change conformation of the looped structures and therefore vary the epitopes 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. 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.
+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. Almost 50% of the variable region’s surface area is exposed on the surface of VlsE. 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]. 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. 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.
 ===Invariable===