SB2013 L04gr5: Difference between revisions

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==''N- and C- Terminal Regions''==  
==''N- and C- Terminal Regions''==  
In addition to the IR6 region, specific sequences of the N- and C- terminal invariable domains are known to be major B cell epitopes in Lyme disease patients. The crystal structure of VlsE indicates that the two sequences lie adjacent to each other, making them a single target covered by peptides VlsE21 through VlsE31 and VlsE336 through VlsE343 (Chandra et al 2011). It has been found that antibodies that interact with this membrane-proximal part become more potent in later stages of infection. According to ELISA results, post Lyme disease syndrome patients exhibited much higher antibody activity at the epitopes than fully recovered patients. Therefore, detection of these antibodies are useful in patient follow-ups, especially with those experiencing the later stages of Lyme disease. (Chandra et al 2011).
In addition to the IR6 region, specific sequences of the N- and C- terminal invariable domains are known to be major B cell epitopes in Lyme disease patients. The crystal structure of VlsE indicates that the two sequences lie adjacent to each other, making them a single target covered by peptides VlsE21 through VlsE31 and VlsE336 through VlsE343.<ref name="Chandra" /> It has been found that antibodies that interact with this membrane-proximal part become more potent in later stages of infection. According to ELISA results, post Lyme disease syndrome patients exhibited much higher antibody activity at the epitopes than fully recovered patients. Therefore, detection of these antibodies are useful in patient follow-ups, especially with those experiencing the later stages of Lyme disease.<ref name="Chandra" />
 
=Conclusion=
=Conclusion=
VlsE is thus an important virulence factor of ''B. burgdorferi''. Through the gene conversion mechanism of the variable regions and the simultaneous protecting of the highly conserved invariable regions, the lipoprotein is able to effectively avoid the antibodies of the host immune system. These roles of VlsE are critical to the survival of the spirochete, as demonstrated by the decreased infectivity of ''B. burgdorferi'' upon the removal of the locus for VlsE.<ref name="Bankhead and Chaconas" />
VlsE is thus an important virulence factor of ''B. burgdorferi''. Through the gene conversion mechanism of the variable regions and the simultaneous protecting of the highly conserved invariable regions, the lipoprotein is able to effectively avoid the antibodies of the host immune system. These roles of VlsE are critical to the survival of the spirochete, as demonstrated by the decreased infectivity of ''B. burgdorferi'' upon the removal of the locus for VlsE.<ref name="Bankhead and Chaconas" />

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Emma Brower, Alexandra DePastene, Olivia Rodrigues, Julia Joseph, Alexander Berchansky, Michal Harel