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In 1968 Shirley Chisholm became the first Black woman elected to the United States Congress. In 1972 she launched a campaign for the Democratic presidential nomination, breaking another political barrier.
MORE →Reflects the personal views, recollections, and perspective of the author, Mike Davis.
This is a personal recollection on the Move fire on May 13, 1985
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major histocompatibility complex, class II, DQ1
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| Haplotypes | DQA1*0101:DQB1*0501 DQA1*0101:DQB1*0502 DQA1*0102:DQB1*0502 DQA1*0104:DQB1*0503 DQA1*0103:DQB1*0601 DQA1*0102:DQB1*0602 DQA1*0103:DQB1*0603 DQA1*0102:DQB1*0604 DQA1*0102:DQB1*0605 DQA1*0102:DQB1*0609.... |
| Structure | |
| Identifiers | alpha 1 *0101 *0102 *0103 *0104
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| Symbol(s) | HLA-DQA1[permanent dead link] |
| EBI-HLA | DQA1*0101 |
| EBI-HLA | DQA1*0102 Archived 2011-05-15 at the Wayback Machine |
| EBI-HLA | DQA1*0103 |
| EBI-HLA | DQA1*0104 |
| Identifiers | beta 1 *05 or *06
|
| Symbol(s) | HLA-DQB1 |
| EBI-HLA | DQB1*05 |
| EBI-HLA | DQB1*06 |
| Shared data | |
| Locus | chr.6 6p21.31 |
HLA-DQ1 is a serotype that covers a broad range of HLA-DQ haplotypes. Historically it was identified as a DR-like alpha chain called DC1;[1] later, it was among 3 types DQw1 (later DQ1, and split into DQ5 and DQ6), DQw2 and DQw3. Of these three serotyping specificities only DQw1 recognized DQ alpha chain.[2] The serotype is positive in individuals who bear the DQA1*01 alleles. The most frequently found within this group are: DQA1*0101, *0102, *0103, and *0104. In the illustration on the right, DQ1 serotyping antibodies recognizes the DQ α (magenta), where antibodies to DQA1* gene products bind variable regions close to the peptide binding pocket.
| DQB1* | DQ5 | DQ1 | DQ6 | Sample |
| allele | % | % | % | size (N) |
| 0501 | 69 | 20 | 2 | 5536 |
| 0502 | 48 | 24 | 15 | 919 |
| 0503 | 58 | 22 | 4 | 1327 |
| 0504 | 59 | 17 | 2 | 48 |
| . | ||||
| DQ6 | DQ1 | DQ5 | N | |
| 0601 | 64 | 23 | 675 | |
| 0602 | 67 | 30 | 1 | 5151 |
| 0603 | 62 | 23 | 2 | 2807 |
| 0604 | 59 | 27 | 2 | 1592 |
| 0605 | 76 | 13 | 358 | |
| 0609 | 48 | 32 | 3 | 149 |
The serotyping efficiency of DQ1 recognition relative to DQ5 and DQ6 is listed below. Since DQ1 recognizes alpha, the DQ5 and DQ6 recognition are to beta chain. Meaning that DQ1 is corecognized with DQ5 and DQ6.
The table to the left shows some of the serotyping efficiencies. Efficient recognition of a genotyped allele approaches 100%. Compared to DQ2 serotyping of DQB1*0201 positive individuals (98%), the efficiency of DQ1 recognition is relatively low and error prone.
For this reason DQ1 serotyping is a poor method of typing for transplantation or disease association prediction or study. Nonetheless, it is still widely used and association purported in the literature.
DQA1*0101 is commonly linked to haplotypes of DQB1*05, the common DQA1*0101:DQB1*0501 haplotype which is part of a broader DR1-DQ1 haplotype.
DQA1*0102 is associated with both DR5 and DR6.
DQA1*0102:DQB1*0502 has a bimodal distribution. It is found in the Philippines in high frequency and on the Mediterranean island of Sardinia.
DQA1*0102:DQB1*0602 is a very common haplotype in Eurasia, with higher frequency in central Asia relative to elsewhere. It is part of a European ancestral haplotype B7-DR15-DQ1 that appears to have expanded asymmetrically into Europe. The A3-B7-DR15-DQ1 haplotype indicates relationships in Eurasia that span from Korea to Ireland, indicating some common ancestry in recent times.
DQA1*0102:DQB1*0604 much less frequently found but spread widely.
DQA1*0103 (*0103) shows a negative (protective) association with many autoimmune disease, this association is apparent in Japanese studies in the *0103:DQB1*0601 haplotype, and in Europe with the *0103:DQB1*0603 haplotype, indicating the protective effect is influenced by the alpha chain of DQ. DQA1*0103 is protective against Behçet's disease,[4][5] pemphigus vulgaris,[6] juvenile diabetes,[7][8] steroid-sensitive nephrotic syndrome,[9] myasthenia gravis[10] coeliac disease[11] multiple sclerosis,[12] chronic active hepatitis C,[13] and Vogt–Koyanagi–Harada syndrome.[14] However, it may predispose carriers to chronic infection such as leprosy,[15] Helicobacter pylori-positive gastric lymphoma,[16] and AIDS.[17]
DQA1*0103:DQB1*0601 is part of a multigene haplotype (DRB1*1502:DRB5*0102:DQA1*0103:DQB1*0601:DPA1*02:DPB1*0901) linked to Takayasu's arteritis in Japanese.[18] Another haplotype, DR8-DQ1 which contains this haplotype may be associated with primary biliary cirrhosis,[19] Graves' disease[20] There is a negative association of this DR15-DQ1 haplotype in Japanese with inflammatory bowel disease.[21]
DQA1*0103:DQB1*0603 is part of a DR-DQ haplotype (DR13-DQ1) that increases for primary sclerosing cholangitis[22][23] The same haplotype shows a negative association with rheumatic heart disease,[24]
DQA1*0104:DQB1*0503 is part of a multigene haplotype DR14-DQ5 that is associated with MuSK positive Myasthenia gravis.
Source: Wikipedia. Article content is retrieved live through the MediaWiki API.
HLA-DQ1 is a serotype that covers a broad range of HLA-DQ haplotypes. Historically it was identified as a DR-like alpha chain called DC1; later, it was among 3 types DQw1 (later DQ1, and split into DQ5 and DQ6), DQw2 and DQw3. Of these three serotyping specificities only DQw1 recognized DQ alpha chain. The serotype is positive in individuals who bear the DQA1*01 alleles. The most frequently found within this group are: DQA1*0101, *0102, *0103, and *0104. In the illustration on the right, DQ1 serotyping antibodies recognizes the DQ α (magenta), where antibodies to DQA1* gene products bind variable regions close to the peptide binding pocket.
A single-domain antibody (sdAb), also known as a Nanobody, is an antibody fragment consisting of a single monomeric variable antibody domain. Like a whole antibody, it is able to bind selectively to a specific antigen. With a molecular weight of only 12–15 kDa, single-domain antibodies (sdAbs) are much smaller than common antibodies (150–160 kDa) which are composed of two heavy protein chains and two light chains, and even smaller than Fab fragments (~50 kDa, one light chain and half a heavy chain) and single-chain variable fragments (~25 kDa, two variable domains, one from a light and one from a heavy chain). The first single-domain antibodies were engineered from heavy-chain antibodies found in camelids at the Université Libre de Bruxelles; these are called VHH fragments. Cartilaginous fish also have heavy-chain antibodies (IgNAR, 'immunoglobulin new antigen receptor'), from which single-domain antibodies called VNAR fragments can be obtained. An alternative approach is to split the dimeric variable domains from common immunoglobulin G (IgG) from humans or mice into monomers. Although most research into single-domain antibodies is currently based on heavy chain variable domains, nanobodies derived from light chains have also been shown to bind specifically to target epitopes. Camelid nanobodies have been shown to be just as specific as antibodies, and in some cases they are more robust. They are easily isolated using the same phage panning procedure used for antibodies, allowing them to be cultured in vitro in large concentrations. The smaller size and single domain make these antibodies easier to transform into bacterial cells for bulk production, making them ideal for research purposes. Single-domain antibodies are being researched for multiple pharmaceutical applications, and have potential for use in the treatment of acute coronary syndrome, cancer, Alzheimer's disease, and COVID-19.
Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively. CDRs are where these molecules bind to their specific antigen and their structure/sequence determines the binding activity of the respective antibody. A set of CDRs constitutes a paratope, or the antigen-binding site. As the most variable parts of the molecules, CDRs are crucial to the diversity of antigen specificities generated by lymphocytes.
Anti-immunoglobulin antibodies are protein that detects other antibodies from an organism. Specifically, anti-immunoglobulin antibodies are created by B-cells as antibodies to bind to other immunoglobulins. Immunoglobulins have two regions: the constant region and the variable region. The constant region is involved in effector function, while the variable region is involved in recognizing and binding to antigens. Anti-immunoglobulin antibodies may bind to either the variable or constant region. Anti-immunoglobulin antibodies are a type of secondary antibody. They are able to detect primary antibodies through multiple methods such as a Western blot, immunohistochemistry, immunofluorescence staining, flow cytometry, and ELISA.
Before the 1921 destruction of Tulsa’s Greenwood District, Black residents had created a remarkable center of business and community life. The district included stores, professional offices, entertainment venues and homes owned by Black citizens. Understanding Greenwood means learning what was built—not only what was burned.
MORE →Mae Jemison, aboard Space Shuttle Endeavour in 1992.
