NMR identification of epitopes of lyme disease antigen OspA to monoclonal antibodies

1998 ◽  
Vol 281 (1) ◽  
pp. 61-67 ◽  
Author(s):  
Xiaolin Huang ◽  
Xiaohua Yang ◽  
Benjamin J. Luft ◽  
Shohei Koide
Keyword(s):  
Monoclonal Antibodies ◽  
Lyme Disease ◽  
Nmr Identification ◽  
Disease Antigen

scholarly journals Pre-exposure Prophylaxis With OspA-Specific Human Monoclonal Antibodies Protects Mice Against Tick Transmission of Lyme Disease Spirochetes

2016 ◽  
Vol 214 (2) ◽  
pp. 205-211 ◽  
Author(s):  
Yang Wang ◽  
Aurélie Kern ◽  
Naomi K. Boatright ◽  
Zachary A. Schiller ◽  
Andrew Sadowski ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Lyme Disease ◽  
Human Monoclonal Antibodies ◽  
Tick Transmission ◽  
Exposure Prophylaxis

Borrelia burgdorferi-Specific Monoclonal Antibodies Derived from Mice Primed with Lyme Disease Spirochete-InfectedIxodes scapularisTicks

2002 ◽  
Vol 21 (3) ◽  
pp. 179-182 ◽  
Author(s):  
M. Lamine Mbow ◽  
Robert D. Gilmore ◽  
Brian Stevenson ◽  
William T. Golde ◽  
Joseph Piesman ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Lyme Disease ◽  
Borrelia Burgdorferi

scholarly journals Crystal Structure of Lyme Disease Antigen Outer Surface Protein C fromBorrelia burgdorferi

2001 ◽  
Vol 276 (13) ◽  
pp. 10010-10015 ◽  
Author(s):  
Christoph Eicken ◽  
Vivek Sharma ◽  
Thomas Klabunde ◽  
Rick T. Owens ◽  
Dagmar S. Pikas ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Lyme Disease ◽  
Outer Surface ◽  
Protein C ◽  
Surface Protein ◽  
Outer Surface Protein ◽  
Disease Antigen

The immunogenicity of Echinococcus granulosus antigen 5 is determined by its post-translational modifications

Parasitology ◽  
2005 ◽  
Vol 131 (5) ◽  
pp. 669-677 ◽  
Author(s):  
C. LORENZO ◽  
J. A. LAST ◽  
G. G. GONZÁLEZ-SAPIENZA
Keyword(s):  
Monoclonal Antibodies ◽  
Human Serum ◽  
Echinococcus Granulosus ◽  
Polypeptide Chain ◽  
Cross Reactivity ◽  
Post Translational Modifications ◽  
Early Introduction ◽  
Native Antigen ◽  
Antigen 5 ◽  
Disease Antigen

Since its early introduction as a marker for the immunodiagnosis of hydatid disease, antigen 5 (Ag5) has been regarded as one of the more relevant antigens of Echinococcus granulosus, and it is still widely used in different confirmation techniques. In this work we prepared 2 recombinant forms of the antigen, namely, rAg5 (corresponding to the unprocessed polypeptide chain of the antigen) and rAg5-38s (corresponding to its 38 kDa subunit). Their antigenicities were compared to that of the native antigen using a human serum collection. There was a major drop in the reactivity of the sera, particularly against rAg5-38s, which was confirmed by analysis of the cross-reactivity of 2 panels of monoclonal antibodies specific for rAg5-38s and the native antigen. Using the chemically deglycosylated native antigen, we demonstrated that the reduced antigenicity of the recombinants is due to the loss of the sugar determinants, and not to their misfolding. Inhibition experiments using phosphorylcholine confirmed that this moiety also contributes to the reactivity of the antigen, but to a much lesser extent. The presence of immunodominant highly cross-reactive glycan moieties in the Ag5 molecule may involve a parasite evasion mechanism.

scholarly journals Structural and molecular analysis of a protective epitope of Lyme disease antigen OspA and antibody interactions

2016 ◽  
Vol 30 (5) ◽  
pp. e2595 ◽  
Author(s):  
Shivender Shandilya ◽  
Nese Kurt Yilmaz ◽  
Andrew Sadowski ◽  
Ejemel Monir ◽  
Zachary A. Schiller ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Molecular Analysis ◽  
Protective Epitope ◽  
Antibody Interactions ◽  
Disease Antigen

Structural identification of a key protective B-cell epitope in lyme disease antigen OspA 1 1Edited by I. A. Wilson

2000 ◽  
Vol 302 (5) ◽  
pp. 1153-1164 ◽  
Author(s):  
Wei Ding ◽  
Xiaolin Huang ◽  
Xiaohua Yang ◽  
John J Dunn ◽  
Benjamin J Luft ◽  
...  
Keyword(s):  
Lyme Disease ◽  
B Cell ◽  
Cell Epitope ◽  
Structural Identification ◽  
B Cell Epitope ◽  
Disease Antigen
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