G15SecL05Tpc3
From Proteopedia
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==Osp-B and Fab Antibody Binding Process== | ==Osp-B and Fab Antibody Binding Process== | ||
| - | <scene name='G15SecL05Tpc3/Not_ours/1'> | + | <scene name='G15SecL05Tpc3/Not_ours/1'>ExampleNotOurs</scene> |
==Related Structures== | ==Related Structures== | ||
| - | + | *[http://www.proteopedia.org/wiki/index.php/1p4p Crystal structure of the C-terminal fragment] | |
==Links== | ==Links== | ||
*[http://www.cdc.gov/lyme/ Lyme Disease] CDC Lyme Disease Webpage | *[http://www.cdc.gov/lyme/ Lyme Disease] CDC Lyme Disease Webpage | ||
Revision as of 16:32, 14 August 2012
Contents |
Outer Surface Protein B (Osp-B) of the Borrelia burgdorferi Spirochete Bacterium
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Introduction
is a primary outer-surface lipoprotein molecule found in the Lyme disease spirochete Borrelia burgdorferi, a molecule essential for the survival of the bacterium. Since its primary function is to serve both as a site of antibody recognition and as the microvillar attachment to the Ixodes scapularis midgut, it is constitutively expressed.
Structure
Significance in Lyme Disease
Lyme disease is a disease of the skin, joints, nervous system and heart caused by the spirochete Borrelia burgdorferi, the signature causative agent of this relapsing fever often transmitted to humans via the bite of the deer tick Ixodes scapularis(Becker, 2005). Of particular interest is the Fab fragment of the monoclonal antibody H6831; when directed against the C-terminus of the outer-surface protein Osp-B, these fragments are bactericidal even in the absence of complements or phagocytes (Sadziene, 1994).
Osp-B and Fab Antibody Binding Process
Related Structures
Links
- Lyme Disease CDC Lyme Disease Webpage
- Borrelia burgdorferi
- Ixodes Dammini
Notes and Literature References
1. Becker, M., Bunikis, J., Lade, B.D, Dunn, J.J., Barbour, A.G., Lawson, C.L. “Structural Investigation of Borrelia burgdorferi OspB, a BactericidalFab Target” The Journal of Biological Chemistry; Vol. 280, No.17, issue of April 29, pp. 17363- 17370, 2005
