Osp17, a novel immunodominant outer surface protein of Borrelia afzelii: recombinant expression in Escherichia coli and its use as a diagnostic antigen for serodiagnosis of Lyme borreliosis

1999 ◽  
Vol 187 (4) ◽  
pp. 213-219 ◽  
Author(s):  
Sigrid Jauris-Heipke ◽  
Birgit Rößle ◽  
Gerhard Wanner ◽  
Christiane Habermann ◽  
Dieter Rössler ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lyme Borreliosis ◽  
Outer Surface ◽  
Recombinant Expression ◽  
Surface Protein ◽  
Borrelia Afzelii ◽  
Expression In Escherichia Coli ◽  
Diagnostic Antigen ◽  
Outer Surface Protein

Outer surface protein E antibody response and its effect on complement factor H binding to OspE in Lyme borreliosis

2008 ◽  
Vol 10 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Jaana Panelius ◽  
Taru Meri ◽  
Ilkka Seppälä ◽  
Miia Eholuoto ◽  
Antti Alitalo ◽  
...  
Keyword(s):  
Antibody Response ◽  
Lyme Borreliosis ◽  
Outer Surface ◽  
Surface Protein ◽  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
Outer Surface Protein

scholarly journals The Dominant Epitope of Borrelia garinii Outer Surface Protein C Recognized by Sera from Patients with Neuroborreliosis Has a Surface-Exposed Conserved Structural Motif

1998 ◽  
Vol 66 (9) ◽  
pp. 4073-4079 ◽  
Author(s):  
Marianne J. Mathiesen ◽  
Arne Holm ◽  
Michael Christiansen ◽  
Jens Blom ◽  
Klaus Hansen ◽  
...  
Keyword(s):  
B Cells ◽  
Lyme Borreliosis ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Terminal Region ◽  
Structural Motif ◽  
High Avidity ◽  
Binding Studies ◽  
Outer Surface Protein

ABSTRACT Epitope mapping of outer surface protein C (OspC) by using sera from patients with neuroborreliosis led to the identification of one single major immunodominant epitope within the C-terminal 10 amino acid residues. Peptide binding studies and alanine replacement scanning of the C-terminal decapeptide, PVVAESPKKP, revealed a critical role for the PKKP sequence and its terminal carboxyl group for the binding of immunoglobulin M (IgM) antibodies from patients with Lyme borreliosis. Electron microscopy of antibody-labeled spirochetes indicated that the C-terminal region is exposed on the surface of the spirochete. Based on homology to proteins of known function, this region most probably adopts a polyproline II-like helix, which is found in surface-exposed structures involved in protein-protein interactions. This structural motif is highly conserved in Borrelia species causing Lyme borreliosis and subjected to purifying selection. We suggest that the abundance of the C-terminal region of OspC on the surface of B. burgdorferi allows a multimeric high-avidity interaction between the spirochete and surface Igs on B cells. The resulting cross-linking of surface Igs on B cells may induce a T-cell-independent B-cell activation without IgM-to-IgG switching, thus explaining the lack of IgG antibodies to OspC in neuroborreliosis.

scholarly journals Expression and secretion of outer surface protein (OSP-A) of Borrelia burgdorferi from Escherichia coli

1993 ◽  
Vol 109 (2-3) ◽  
pp. 297-301 ◽  
Author(s):  
Yung-Fu Chang ◽  
Tsai-Ling Lauderdale ◽  
Woo Y. Lee ◽  
Sang J. Shin ◽  
Richard H. Jacobson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Borrelia Burgdorferi ◽  
Outer Surface ◽  
Surface Protein ◽  
Outer Surface Protein
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