G15SecL05Tpc3

From Proteopedia

Revision as of 16:33, 14 August 2012

Outer Surface Protein B (Osp-B) of the Borrelia burgdorferi Spirochete Bacterium

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

• Crystal structure of the C-terminal fragment
• OspB-H6831 Complex
• CB2

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