Complement Regulator-Acquiring Surface Protein: Difference between revisions
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== '''Introduction''' == | == '''Introduction''' == | ||
Lyme disease is caused by the spirochete ''Borrelia burgdorferi'', and is transferred into vertebrate hosts by zoonotic vectors such as ''Ixodes'' ticks (Bykowski et al. 2007). There are thousands of cases of Lyme disease reported each year, making it a prevalent disease in North America and Eurasia (Cordes et al. 2005). In order for ''B. burgdorferi'' to survive in its host, it evades | Lyme disease is caused by the spirochete ''Borrelia burgdorferi'', and is transferred into vertebrate hosts by zoonotic vectors such as ''Ixodes'' ticks (Bykowski et al. 2007). There are thousands of cases of Lyme disease reported each year, making it a prevalent disease in North America and Eurasia (Cordes et al. 2005). In order for ''B. burgdorferi'' to survive in its host, it evades the host's immune system through the use of complement regulator-acquiring surface proteins. One such protein responsible for a successful initial infection is ''Borrelia burgdorferi'' complement regulator-acquiring surface protein 1, or BbCRASP-1 (Bykowski et al. 2007). Because BbCRASP-1 binds host complement regulators to the spirochete's outer surface, ''B. burgdorferi'' remains undetected within the host (Bykowski et al. 2007). BbCRASP-1 specifically binds to complement Factor H (FH) and Factor H-like proteins (FHL-1), which are responsible for the host's immune response and detection of pathogens (Kraiczy et al. 2004). Recently, it was found that BbCRASP-1 binds to several other proteins in the extra cellular matrix of a human cell. | ||
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== '''Function''' == | == '''Function''' == | ||
Bb CRASP-1 can be found on the outer layer of the Lyme disease spirochete and | Bb CRASP-1 can be found on the outer layer of the Lyme disease spirochete and is essential for the infiltration of the spirochete into the host (Bykowski 2007). BbCRASP-1 provides resistance for the spirochete against the host's complementary immune system as well as spreading of the spirochete within the host. | ||
=== '''Host Immune Response Evasion''' === | === '''Host Immune Response Evasion''' === | ||
BbCRASP-1 has an affinity for | BbCRASP-1 has an affinity for Factor H and Factor H-like proteins. Therefore, Factor H binds to BbCRASP-1, which is bound to the outer surface of the spirochete. Because there are multiple BbCRASP-1 proteins on the spirochete, the spirochete is coated with [http://www.uniprot.org/uniprot/CFAH_HUMAN Factor H] and effectively able to infiltrate the host and go undetected in the host's plasma(Bykowski 2007). | ||
=== '''Relation to the Extra Cellular Matrix''' === | === '''Relation to the Extra Cellular Matrix''' === | ||
Recently it was found that BbCRASP-1 not only binds to FH and FHL-1 proteins, but it also binds to several other human ligands such as [http://www.uniprot.org/uniprot/BMP2_HUMAN BMP-2] and Extra cellular matrix ligands Collagen I, Collagen III, Collagen IV, fibronectin, laminin, and plasminogen (Hallstrom et al. 2010). As a result of this new finding, BbCRASP-1 is said to advocate the bypassing of the complementary immune system in addition to the pathogenesis of Lyme disease. BbCRASP-1 facilitates binding of “Borrelia burgdoferi” to human cells and tissues, which helps spread the infection (Hallstrom et al. 2010). | |||
