G15SecL05Tpc3

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<Structure load='1rjl' size='500' frame='true' align='right' caption='Osp-B Structure' scene='Insert optional scene name here' />
<Structure load='1rjl' size='500' frame='true' align='right' caption='Osp-B Structure' scene='Insert optional scene name here' />
==Introduction==
==Introduction==
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<scene name='G15SecL05Tpc3/Ospb/1'>Osp-B</scene> is an outer-surface protein 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.
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<scene name='G15SecL05Tpc3/Ospb/1'>Osp-B</scene> 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==
==Structure==
==Significance in Lyme Disease==
==Significance in Lyme Disease==
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Lyme disease is a disease of the skin, joints, nervous system and heart caused by the spirochete ''Borrelia burgdorferi'', the signature causative agent of the 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, a primary lipoprotein of the burgdorferi spirochete, these fragments are bactericidal even in the absence of complements or phagocytes (Sadziene, 1994).
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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==
==Osp-B and Fab Antibody Binding Process==

Revision as of 15:32, 14 August 2012

Contents

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

Osp-B Structure

Drag the structure with the mouse to rotate

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

Links


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

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Michael Pape, Farbod Raegan, Michal Harel

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