SB2013 L08gr01: Difference between revisions

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==Immune Response==

However, the existence of the negatively charged region may not be the only reason contributing the invasion. Overall structure of OspC may play an equally important role. Recent studies showed that, in serum of patients demonstrating erythema migrans (early stage of Lyme disease), IgM antibody has been found to interact with OspC <ref>Wilske B, Preac-Mursic V, Schierz G, Busch K. Immunochemical and immunological analysis of European Borrelia burgdorferi strains. 1986. Zentralbl Bakteriol Mikrobiol Hyg A. Vol. 263, No. 1-2. 10 p.</ref>. On the other hand, immunoblot of serum from patients showing secondary infection has been observed to demonstrate a lower number of IgM-OspC complexes, further demonstrating the importance of OspC for the primary transmission <ref>Dressler F, Whalen J, Reinhardt B, Steere A. Western blotting in the serodiagnosis of Lyme disease. 1993. J Clin Microbiol. Vol. 167. 8 p.</ref>. In addition, moderate IgG reactivity to OspC has been found in the serum of patients at an early stage of Lyme disease <ref>Fung B, McHugh G, Leong J, Steere A. Humoral immune response to outer surface protein C of Borrelia burgdorferi in Lyme disease: role of the immunoglobulin M response in the serodiagnosis of early infection. 1994. Infection and Immunity. Vol. 62. 8 p.</ref>. Furthermore, supporting researches have highlighted a well-conserved immunodominant epitope located on the <scene name='Talk:SB2013_L08gr1/C-terminus/1'>carboxy-terminal</scene> region of OspC demonstrating the ability of binding to antibodies <ref name="jobe">Jobe D, Lovrich S, Schell R, Callister S. C-terminal region of outer surface protein C binds borreliacidal antibodies in sera from patients with Lyme disease. 2003. Clin Vaccine immuno.Vol. 10. 5 p.</ref>. IgM and IgG antibodies from serum of patients at an early stage of Lyme disease get absorbed with a carboxy-terminal (seven amino acid long) of OspC. Surprisingly, this epitope on the carboxy-terminal and its binding of antibodies is very well conserved among different invasive OspC proteins <ref>Lovrich S, Jobe D, Schell R, Callister S. Borreliacidal OspC antibodies specific for a highly conserved epitope are immunodominant in human Lyme disease and do not occur in mice or hamsters. 2005. Clin Vaccine Immuno. Vol. 12. 6 p.</ref>.

However, the existence of the negatively charged region may not be the only reason contributing the invasion. Overall structure of OspC may play an equally important role. Recent studies showed that, in serum of patients demonstrating erythema migrans (early stage of Lyme disease),IgM [[Immunoglobulin M]] antibody has been found to interact with OspC <ref>Wilske B, Preac-Mursic V, Schierz G, Busch K. Immunochemical and immunological analysis of European Borrelia burgdorferi strains. 1986. Zentralbl Bakteriol Mikrobiol Hyg A. Vol. 263, No. 1-2. 10 p.</ref>. On the other hand, immunoblot of serum from patients showing secondary infection has been observed to demonstrate a lower number of IgM-OspC complexes, further demonstrating the importance of OspC for the primary transmission <ref>Dressler F, Whalen J, Reinhardt B, Steere A. Western blotting in the serodiagnosis of Lyme disease. 1993. J Clin Microbiol. Vol. 167. 8 p.</ref>. In addition, moderate IgG reactivity to OspC has been found in the serum of patients at an early stage of Lyme disease <ref>Fung B, McHugh G, Leong J, Steere A. Humoral immune response to outer surface protein C of Borrelia burgdorferi in Lyme disease: role of the immunoglobulin M response in the serodiagnosis of early infection. 1994. Infection and Immunity. Vol. 62. 8 p.</ref>. Furthermore, supporting researches have highlighted a well-conserved immunodominant epitope located on the <scene name='Talk:SB2013_L08gr1/C-terminus/1'>carboxy-terminal</scene> region of OspC demonstrating the ability of binding to antibodies <ref name="jobe">Jobe D, Lovrich S, Schell R, Callister S. C-terminal region of outer surface protein C binds borreliacidal antibodies in sera from patients with Lyme disease. 2003. Clin Vaccine immuno.Vol. 10. 5 p.</ref>. IgM and IgG antibodies from serum of patients at an early stage of Lyme disease get absorbed with a carboxy-terminal (seven amino acid long) of OspC. Surprisingly, this epitope on the carboxy-terminal and its binding of antibodies is very well conserved among different invasive OspC proteins <ref>Lovrich S, Jobe D, Schell R, Callister S. Borreliacidal OspC antibodies specific for a highly conserved epitope are immunodominant in human Lyme disease and do not occur in mice or hamsters. 2005. Clin Vaccine Immuno. Vol. 12. 6 p.</ref>.

==Super Vaccination==

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 ==Immune Response==
-However, the existence of the negatively charged region may not be the only reason contributing the invasion. Overall structure of OspC may play an equally important role. Recent studies showed that, in serum of patients demonstrating erythema migrans (early stage of  Lyme disease), IgM antibody has been found to interact with OspC <ref>Wilske B, Preac-Mursic V, Schierz G, Busch K. Immunochemical and immunological analysis	of European Borrelia burgdorferi strains. 1986. Zentralbl Bakteriol Mikrobiol Hyg A.	Vol. 263, No. 1-2. 10 p.</ref>. On the other hand, immunoblot of serum from patients showing secondary infection has been observed to demonstrate a lower number of IgM-OspC complexes, further demonstrating the importance of OspC for the primary transmission <ref>Dressler F, Whalen J, Reinhardt B, Steere A. Western blotting in the serodiagnosis of Lyme	disease. 1993. J Clin Microbiol. Vol. 167. 8 p.</ref>. In addition, moderate IgG reactivity to OspC has been found in the serum of patients at an early stage of Lyme disease <ref>Fung B, McHugh G, Leong J, Steere A. Humoral immune response to outer surface protein C of Borrelia burgdorferi in Lyme disease: role of the immunoglobulin M response in the serodiagnosis of early infection. 1994. Infection and Immunity. Vol. 62. 8 p.</ref>. Furthermore, supporting researches have highlighted a well-conserved  immunodominant epitope located on the <scene name='Talk:SB2013_L08gr1/C-terminus/1'>carboxy-terminal</scene> region of OspC demonstrating the ability of binding to antibodies <ref name="jobe">Jobe D, Lovrich S, Schell R, Callister S. C-terminal region of outer surface protein C binds	borreliacidal antibodies in sera from patients with Lyme disease. 2003. Clin Vaccine immuno.Vol. 10. 5 p.</ref>. IgM and IgG antibodies from serum of patients at an early stage of Lyme disease get absorbed with a carboxy-terminal (seven amino acid long) of OspC. Surprisingly, this epitope on the carboxy-terminal and its binding of antibodies is very well conserved among different invasive OspC proteins <ref>Lovrich S, Jobe D, Schell R, Callister S. Borreliacidal OspC antibodies specific for a highly conserved epitope are immunodominant in human Lyme disease and do not occur in mice	or hamsters. 2005. Clin Vaccine Immuno. Vol. 12. 6 p.</ref>.
+However, the existence of the negatively charged region may not be the only reason contributing the invasion. Overall structure of OspC may play an equally important role. Recent studies showed that, in serum of patients demonstrating erythema migrans (early stage of  Lyme disease),IgM [[Immunoglobulin M]] antibody has been found to interact with OspC <ref>Wilske B, Preac-Mursic V, Schierz G, Busch K. Immunochemical and immunological analysis	of European Borrelia burgdorferi strains. 1986. Zentralbl Bakteriol Mikrobiol Hyg A.	Vol. 263, No. 1-2. 10 p.</ref>. On the other hand, immunoblot of serum from patients showing secondary infection has been observed to demonstrate a lower number of IgM-OspC complexes, further demonstrating the importance of OspC for the primary transmission <ref>Dressler F, Whalen J, Reinhardt B, Steere A. Western blotting in the serodiagnosis of Lyme	disease. 1993. J Clin Microbiol. Vol. 167. 8 p.</ref>. In addition, moderate IgG reactivity to OspC has been found in the serum of patients at an early stage of Lyme disease <ref>Fung B, McHugh G, Leong J, Steere A. Humoral immune response to outer surface protein C of Borrelia burgdorferi in Lyme disease: role of the immunoglobulin M response in the serodiagnosis of early infection. 1994. Infection and Immunity. Vol. 62. 8 p.</ref>. Furthermore, supporting researches have highlighted a well-conserved  immunodominant epitope located on the <scene name='Talk:SB2013_L08gr1/C-terminus/1'>carboxy-terminal</scene> region of OspC demonstrating the ability of binding to antibodies <ref name="jobe">Jobe D, Lovrich S, Schell R, Callister S. C-terminal region of outer surface protein C binds	borreliacidal antibodies in sera from patients with Lyme disease. 2003. Clin Vaccine immuno.Vol. 10. 5 p.</ref>. IgM and IgG antibodies from serum of patients at an early stage of Lyme disease get absorbed with a carboxy-terminal (seven amino acid long) of OspC. Surprisingly, this epitope on the carboxy-terminal and its binding of antibodies is very well conserved among different invasive OspC proteins <ref>Lovrich S, Jobe D, Schell R, Callister S. Borreliacidal OspC antibodies specific for a highly conserved epitope are immunodominant in human Lyme disease and do not occur in mice	or hamsters. 2005. Clin Vaccine Immuno. Vol. 12. 6 p.</ref>.
 ==Super Vaccination==