G15SecL05Tpc3: Difference between revisions

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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==
<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.
<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.
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==Significance in Lyme Disease==
==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).   
Lyme disease is an bacterial infectious disease of the skin, joints, nervous system and heart caused by the spirochete ''Borrelia burgdorferi'', 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==
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==Notes and Literature References==
==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
*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
2. Connolly, S.E., Benach, J.L. “The Versatile Roles of Antibodies in Borrelia Infections” Nature Reviews: Microbiology, Volume 3, May 2005, pp. 411-420
*2. Connolly, S.E., Benach, J.L. “The Versatile Roles of Antibodies in Borrelia Infections” Nature Reviews: Microbiology, Volume 3, May 2005, pp. 411-420