Difference between revisions of "Part:BBa K3767004"
Victor5688 (Talk | contribs) |
|||
Line 6: | Line 6: | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
− | Outer surface protein A (OspA) is an abundant lipoprotein that resides on the bacterium Borrelia Burgfedori (Borrelia meaning invasive spiral shaped pathogen), which is carried by ticks and transmitted via a tick bite. Borrelia Burgfedori | + | Outer surface protein A (OspA) is an abundant lipoprotein that resides on the bacterium Borrelia Burgfedori (Borrelia meaning invasive spiral shaped pathogen), which is carried by ticks and transmitted via a tick bite. Borrelia Burgfedori expresses the protein OspA, which plays a role in the attachment and penetration of the spirochete to the epithelial cells once bitten by the tick[[Part:BBa_K3767004#References|<sup>[1]</sup>]]. The amino acid sequence of OspA begins with residues believed to function as signal sequences for transport, proteolytic processing and lipidation[[Part:BBa_K3767004#References|<sup>[2]</sup>]]. [[File:BBa K3767004 OspA colored.png|300px|right|thumb| Figure 1. Colored model of purified OspA from E.Coli.]]Recent findings have also shown that OspA is important in the inflammation process in Lyme disease, thus possesses both B-cell mitogenic effect and a cytokine-stimulatory effect[[Part:BBa_K3767004#References|<sup>[1]</sup>]]. |
OspA is composed with a prolonged fold with 21 anti-parallel beta sheets and a single alpha helix, which are arranged to form the N-terminal, central sheet and C-terminal [[Part:BBa_K3767004#References|<sup>[3]</sup>]]. OspA has a unique folding pattern that includes alternating charge arrays into anti-parallel β-sheet, a potential ligand binding site and a distinctive variable motif [[Part:BBa_K3767004#References|<sup>[3]</sup>]]. OspA normally has a lipidated N-terminal cysteine, a recombinant unlipidated form is soluble in aqueous solution and is still recognized by antibodies from Lyme Disease | OspA is composed with a prolonged fold with 21 anti-parallel beta sheets and a single alpha helix, which are arranged to form the N-terminal, central sheet and C-terminal [[Part:BBa_K3767004#References|<sup>[3]</sup>]]. OspA has a unique folding pattern that includes alternating charge arrays into anti-parallel β-sheet, a potential ligand binding site and a distinctive variable motif [[Part:BBa_K3767004#References|<sup>[3]</sup>]]. OspA normally has a lipidated N-terminal cysteine, a recombinant unlipidated form is soluble in aqueous solution and is still recognized by antibodies from Lyme Disease |
Revision as of 16:40, 5 July 2021
Outer Surface Protein A (OspA) from Borrelia Burgdorferi
Current Lyme disease testing involves Enzyme-linked immunosorbent assay (ELISA) test which is used to detect Borrelia Burgfedori antibodies after a tick bite. However, by testing for OspA on the tick itself, we hope to be able to identify an earlier diagnosis for the Borrelia Burgfedori bacterium in the case of a tick bite.
Usage and Biology
Outer surface protein A (OspA) is an abundant lipoprotein that resides on the bacterium Borrelia Burgfedori (Borrelia meaning invasive spiral shaped pathogen), which is carried by ticks and transmitted via a tick bite. Borrelia Burgfedori expresses the protein OspA, which plays a role in the attachment and penetration of the spirochete to the epithelial cells once bitten by the tick[1]. The amino acid sequence of OspA begins with residues believed to function as signal sequences for transport, proteolytic processing and lipidation[2]. Recent findings have also shown that OspA is important in the inflammation process in Lyme disease, thus possesses both B-cell mitogenic effect and a cytokine-stimulatory effect[1].OspA is composed with a prolonged fold with 21 anti-parallel beta sheets and a single alpha helix, which are arranged to form the N-terminal, central sheet and C-terminal [3]. OspA has a unique folding pattern that includes alternating charge arrays into anti-parallel β-sheet, a potential ligand binding site and a distinctive variable motif [3]. OspA normally has a lipidated N-terminal cysteine, a recombinant unlipidated form is soluble in aqueous solution and is still recognized by antibodies from Lyme Disease
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
1. Hansson, L., Noppa, L., Nilsson, A., Stromqvist, M., Bergstrom, S. (1994). Expression of Truncated and Full-Length Forms of the Lyme Disease Borrelia Outer Surface Protein A in Escherichia coli, Umed University, Umed, Sweden.
2. Dunn, J., Lade, B., Barbour, A. (1990). Outer Surface Protein A (OspA) from Lyme Disease Spirochete, Borrelia burgdorferi: High Level Expression and Purification of a Soluble Recombinant from of OspA, University of Texas, San Antonio, Texas.
3. Park, J., Prilusky, J., Harel, M and Martz, E. (2015). OspA. Proteopedia [Online].https://proteopedia.org/wiki/index.php/OspA. (Accessed June 19, 2022).
4. Chang, Y-F., Lauderdale, T-L., Lee, W., Shin, J., Jacobson, R., Appel, M and Lein, D. (1993). Expression and secretion of outer surface protein (OSP-A) of Borrelia burgdorferi from Escherichia coli, Cornell University, Ithaca, NY, USA.