G15SecL05Tpc3: Difference between revisions

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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.

<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. Variation in the synthesis of Osp-B and other outer surface proteins is the means by which B. burgdorferi evades the host immune system and adapts to various host microenvironments, such as those in the common tick vector. B. burgdorferi selectively expresses specific Osps in distinct phases of its life cycle and in specific tissue locations: expression of B. burgdorferi OspB is immediately turned on when the spirochetes enter and reside within the tick vector. However, during transmission from the arthropod vector to a vertebrate host, B. burgdorferi down-regulates OspB expression and up-regulates the expression of proteins such as OspC, DbpA, and BBK32. This selective gene expression of Osp-B and other proteins in ticks suggests that these two proteins may function during early spirochete colonization and persistence within the tick vector (Cite).

==Significance in Lyme Disease and Bind Briefing==

G15SecL05Tpc3: Difference between revisions

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Revision as of 04:47, 15 August 2012 view source Michael Pape (talk \| contribs) 72 edits No edit summary ← Older edit		Revision as of 05:34, 15 August 2012 view source Michael Pape (talk \| contribs) 72 edits No edit summary Newer edit →
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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.		<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. Variation in the synthesis of Osp-B and other outer surface proteins is the means by which B. burgdorferi evades the host immune system and adapts to various host microenvironments, such as those in the common tick vector. B. burgdorferi selectively expresses specific Osps in distinct phases of its life cycle and in specific tissue locations: expression of B. burgdorferi OspB is immediately turned on when the spirochetes enter and reside within the tick vector. However, during transmission from the arthropod vector to a vertebrate host, B. burgdorferi down-regulates OspB expression and up-regulates the expression of proteins such as OspC, DbpA, and BBK32. This selective gene expression of Osp-B and other proteins in ticks suggests that these two proteins may function during early spirochete colonization and persistence within the tick vector (Cite).

	==Significance in Lyme Disease and Bind Briefing==		==Significance in Lyme Disease and Bind Briefing==