SB2013 L04gr5: Difference between revisions
Emma Brower (talk | contribs) No edit summary |
Emma Brower (talk | contribs) No edit summary |
||
| Line 10: | Line 10: | ||
The lipoprotein, VlsE, consists of two invariable domains at the amino and carboxyl termini and a variable domain (Figure 1). When referring to the primary structure of the protein, the variable domain is a cassette region located between the two termini. The variable domain can be further broken down into variable regions (<scene name='SB2013_L04gr5/Variable_regions/3'>VRs</scene>) and invariable regions (<scene name='SB2013_L04gr5/Invariable_regions/2'>IRs</scene>) (Liang et al. 1999). | The lipoprotein, VlsE, consists of two invariable domains at the amino and carboxyl termini and a variable domain (Figure 1). When referring to the primary structure of the protein, the variable domain is a cassette region located between the two termini. The variable domain can be further broken down into variable regions (<scene name='SB2013_L04gr5/Variable_regions/3'>VRs</scene>) and invariable regions (<scene name='SB2013_L04gr5/Invariable_regions/2'>IRs</scene>) (Liang et al. 1999). | ||
When crystallized, VlsE forms a four molecule asymmetric unit | When crystallized, VlsE forms a four molecule asymmetric unit with each molecule having slight differences in their conformation. Although each molecule in the unit is slightly different, a single molecule of the protein consists of eleven [http://en.wikipedia.org/wiki/Alpha_helices α-helices] and four short [http://en.wikipedia.org/wiki/Beta_strand β-strands]. Helices α1 (aa 306-341), α2 (aa 68-87), α3 (aa 114-139), and α11 (aa 306-341) all form the <scene name='SB2013_L04gr5/Membrane_proximal_region/1'>membrane proximal region</scene> of VlsE, while helices α4 through α10 form the primary region of the <scene name='SB2013_L04gr5/Membrane_distal_region/2'>membrane distal region</scene> of the protein. The four short β-strands each consist of 3 amino acids and can also be located in the membrane distal region. | ||
Covering the membrane distal part of VlsE are connecting loop regions, which lack secondary structure and have different conformations in each of the molecules. (Eicken et al. 2002). Helices α3 through α10 form the invariable regions and are attached by the connecting loops that are classified as the variable regions. Although VlsE crystallizes into an asymmetrical unit, it appears primarily as monomeric in solution. Because the interface between VlsE molecules in the crystal structure buries approximately 13% of the accessible surface area of the monomers, Eicken et al.suggest that there is a possibility of VlsE existing as a [http://en.wikipedia.org/wiki/Protein_dimer dimer] when in its natural state (Figure 2). <scene name='SB2013_L04gr5/Reset_button/1'>Reset</scene> | Covering the membrane distal part of VlsE are connecting loop regions, which lack secondary structure and have different conformations in each of the molecules. (Eicken et al. 2002). Helices α3 through α10 form the invariable regions and are attached by the connecting loops that are classified as the variable regions. Although VlsE crystallizes into an asymmetrical unit, it appears primarily as monomeric in solution. Because the interface between VlsE molecules in the crystal structure buries approximately 13% of the accessible surface area of the monomers, Eicken et al.suggest that there is a possibility of VlsE existing as a [http://en.wikipedia.org/wiki/Protein_dimer dimer] when in its natural state (Figure 2). <scene name='SB2013_L04gr5/Reset_button/1'>Reset</scene> | ||
| Line 61: | Line 61: | ||
3.<ref name="CDC">[http://www.cdc.gov/lyme/transmission/index.html http://www.cdc.gov/lyme/transmission/index.html]</ref> | 3.<ref name="CDC">[http://www.cdc.gov/lyme/transmission/index.html http://www.cdc.gov/lyme/transmission/index.html]</ref> | ||
4.<ref name="Liang">Liang F, Philipp M. 1999. Analysis of Antibody Response to Invariable Regions of VlsE,The Variable Surface Antigen of ''Borrelia burgdorferi''. Infection and Immunity. 6702-6706. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/?term=10569796 10569796]</ref> | 4.<ref name="Liang">Liang F, Philipp M. 1999. Analysis of Antibody Response to Invariable Regions of VlsE,The Variable Surface Antigen of ''Borrelia burgdorferi''. Infection and Immunity. 6702-6706. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/?term=10569796 10569796]</ref> | ||
5. | |||
6.<ref name="Zhang and Norris"> Zhang J, Norris S. 1998. Genetic Variation of the ''Borrelia burgdorferi'' Gene ''VlsE'' Involves Cassette-Specific, Segmental Gene Conversion. Infection and Immunity. 66(8): 3698-3704. [http://www.ncbi.nlm.nih.gov/pubmed/9673251 9673251]</ref> | |||
9.<ref name="Liang B">Liang F, Steere A, Marques A, Johnson B, Miller J, Philipp M. 1999. Sensitive and Specific Serodiagnosis of Lyme Disease by Enzyme-Linked Immunosorbent Assay with a Peptide Based on an Immunodominant Conserved Region of ''Borrelia burgdorferi'' VlsE. Journal of Clinical Microbiology.37(12): 3990-3996. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10565920 10565920]</ref> | 9.<ref name="Liang B">Liang F, Steere A, Marques A, Johnson B, Miller J, Philipp M. 1999. Sensitive and Specific Serodiagnosis of Lyme Disease by Enzyme-Linked Immunosorbent Assay with a Peptide Based on an Immunodominant Conserved Region of ''Borrelia burgdorferi'' VlsE. Journal of Clinical Microbiology.37(12): 3990-3996. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10565920 10565920]</ref> | ||
10.<ref name="Chandra">Chandra A, Latov N, Wormser G, Marques A, Alaedini A. 2011. Epitope mapping of antibodies to VlsE protein of ''Borrelia burgdorferi'' in post-Lyme disease syndrome. Clinical Immunology. 141(1): 103-110. PMID[http://www.ncbi.nlm.nih.gov/pubmed/21778118 21778118]</ref> | 10.<ref name="Chandra">Chandra A, Latov N, Wormser G, Marques A, Alaedini A. 2011. Epitope mapping of antibodies to VlsE protein of ''Borrelia burgdorferi'' in post-Lyme disease syndrome. Clinical Immunology. 141(1): 103-110. PMID[http://www.ncbi.nlm.nih.gov/pubmed/21778118 21778118]</ref> | ||