SB2013 L04gr5: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 29: Line 29:
<scene name='SB2013_L04gr5/Ir6/1'>IR6</scene>, the second least exposed region composed of 26 amino acids, has been found to be the most conserved IR and the most immunogenic as observed in studies involving monkeys and humans.  In a study conducted by Liang et al., serum samples from monkeys were infected by the bite of ''Ixodes scapularis'' nymphal ticks. The results showed a robust response to IR6 and little to no response to the remaining IRs. Similarly, only IR6 elicited a strong immune response in infected humans. Clearly, due to its highly conserved structure and immunodominance, IR6 is important to the functionality of ''B. Burgdorferi'' and therefore requires its strategic placement indicated in the crystallized structure (Eicken et al 2002). In mice, however, a strong response was detected across IRs 6, 2, and 4, but not in IRs 1, 3, and 5. (Liang et al 1999 A), thus demonstrating the importance of IR6 across many species and indicating that further research into the fuctions of IRs 2 and 4 is needed.   
<scene name='SB2013_L04gr5/Ir6/1'>IR6</scene>, the second least exposed region composed of 26 amino acids, has been found to be the most conserved IR and the most immunogenic as observed in studies involving monkeys and humans.  In a study conducted by Liang et al., serum samples from monkeys were infected by the bite of ''Ixodes scapularis'' nymphal ticks. The results showed a robust response to IR6 and little to no response to the remaining IRs. Similarly, only IR6 elicited a strong immune response in infected humans. Clearly, due to its highly conserved structure and immunodominance, IR6 is important to the functionality of ''B. Burgdorferi'' and therefore requires its strategic placement indicated in the crystallized structure (Eicken et al 2002). In mice, however, a strong response was detected across IRs 6, 2, and 4, but not in IRs 1, 3, and 5. (Liang et al 1999 A), thus demonstrating the importance of IR6 across many species and indicating that further research into the fuctions of IRs 2 and 4 is needed.   
   
   
The high immunogenicity effect of IR6 is thought to only occur in dead bacteria due to its low maximal theoretical surface exposure in living ''B. borgderfuri'' (13.7%). Interaction with anti-IR6 antibodies would be limited to the exposed <scene name='SB2013_L04gr5/Ir6_residues/1'>amino acid residues</scene>, Lys-274, Gln-279, Lys-291,Lys-294 (Eicken). These amino acids would be the likely targets of the host immune response.  The immunodominant nature of VlsE, especially in IR6, makes it a viable diagnostic tool (Marangoni).
The high immunogenicity effect of IR6 is thought to only occur in dead bacteria due to its low maximal theoretical surface exposure in living ''B. borgderfuri'' (13.7%). Interaction with anti-IR6 antibodies would be limited to the exposed <scene name='SB2013_L04gr5/Ir6_residues/1'>amino acid residues</scene>, Lys-274, Gln-279, Lys-291,Lys-294 (Eicken). These amino acids would be the likely targets of the host immune response.  The immunodominant nature of VlsE, especially in IR6, makes it a viable diagnostic tool.<ref name="Marangoni" />


<scene name='SB2013_L04gr5/Reset_original/2'>Reset Structure</scene>  
<scene name='SB2013_L04gr5/Reset_original/2'>Reset Structure</scene>  
Line 35: Line 35:
=VlsE as a Diagnostic Tool=
=VlsE as a Diagnostic Tool=
== ''IR 6''==
== ''IR 6''==
IR6 is instrumental in the serodiagnosis of Lyme disease in its early stages. The sensitivity and precision of ELISA was measured based on a 26-mer synthetic peptide (C6) whose sequence matched that of IR6 (Marangoni et al 2006). Serum samples in nonhuman primates that were introduced to different strains of ''B. burgdorferi'' were assessed for antibody responses. Antibody  [http://en.wikipedia.org/wiki/Immunoglobulin_G IgG]was present in high levels for all animals over a 160-week period following infection. Human patients assessed with the C6 ELISA yielded 74% detection sensitivity in the acute disease type, 90% in the convalescent (recovery) phase, 95% in the early disseminated phase, and 100% in late Lyme disease. No antibody responses to peptides resembling the sequences of the remaining IRs were detected in humans or monkeys (Liang et al 1999 B).
IR6 is instrumental in the serodiagnosis of Lyme disease in its early stages. The sensitivity and precision of ELISA was measured based on a 26-mer synthetic peptide (C6) whose sequence matched that of IR6.<ref name="Marangoni" /> Serum samples in nonhuman primates that were introduced to different strains of ''B. burgdorferi'' were assessed for antibody responses. Antibody  [http://en.wikipedia.org/wiki/Immunoglobulin_G IgG]was present in high levels for all animals over a 160-week period following infection. Human patients assessed with the C6 ELISA yielded 74% detection sensitivity in the acute disease type, 90% in the convalescent (recovery) phase, 95% in the early disseminated phase, and 100% in late Lyme disease. No antibody responses to peptides resembling the sequences of the remaining IRs were detected in humans or monkeys (Liang et al 1999 B).


==''N- and C- Terminal Regions''==  
==''N- and C- Terminal Regions''==  
Line 59: Line 59:
9.<ref name="Liang B">Liang F, Steere A, Marques A, Johnson B, Miller J, Philipp M. 1999. Sensitive and Specific Serodiagnosis of Lyme Disease by Enzyme-Linked Immunosorbent Assay with a Peptide Based on an Immunodominant Conserved Region of ''Borrelia burgdorferi'' VlsE. Journal of Clinical Microbiology.37(12): 3990-3996. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10565920 10565920]</ref>
9.<ref name="Liang B">Liang F, Steere A, Marques A, Johnson B, Miller J, Philipp M. 1999. Sensitive and Specific Serodiagnosis of Lyme Disease by Enzyme-Linked Immunosorbent Assay with a Peptide Based on an Immunodominant Conserved Region of ''Borrelia burgdorferi'' VlsE. Journal of Clinical Microbiology.37(12): 3990-3996. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10565920 10565920]</ref>
10.<ref name="Chandra">Chandra A, Latov N, Wormser G, Marques A, Alaedini A. 2011. Epitope mapping of antibodies to VlsE protein of ''Borrelia burgdorferi'' in post-Lyme disease syndrome. Clinical Immunology. 141(1): 103-110. PMID[http://www.ncbi.nlm.nih.gov/pubmed/21778118 21778118]</ref>  
10.<ref name="Chandra">Chandra A, Latov N, Wormser G, Marques A, Alaedini A. 2011. Epitope mapping of antibodies to VlsE protein of ''Borrelia burgdorferi'' in post-Lyme disease syndrome. Clinical Immunology. 141(1): 103-110. PMID[http://www.ncbi.nlm.nih.gov/pubmed/21778118 21778118]</ref>  
11.<ref name="Marangoni">Marangoni A, Sambri V, Accardo S, Cavrini F, Mondardini V, Moroni A, Storni E, Cevenini R. 2006. A Decrease in the Immunoglobulin G Antibody Response Against against the VlsE Protein of Borrelia burgdorferi Sensu Lato Correlates with the Resolution of Clinical Signs in Antibiotic-Treated Patients with Early Lyme Disease. Clinical and Vaccine Immunology. 13(4): 525-529. PMID[http://www.ncbi.nlm.nih.gov/pubmed/16603623 16603623]</ref>


</ref>
</ref>
}}
}}
Retrieved from "https://proteopedia.org/SB2013_L04gr5"