Disease relevance of IGKV3-20

• In contrast, treatment of A27/80 and OVCAR-3 epithelial ovarian cancer cells with IFNgamma stimulated H-REV107-1 expression [1].
• METHODS: Priming of blood eosinophils obtained from patients with allergy and donors without allergy was measured by labeling with monoclonal phage antibodies A17 and A27 recognizing priming-associated epitopes on phagocytes [2].
• Immunofluorescent staining determined that the distance traveled by A27-deficient virions was sufficient for transport to the site of envelopment [3].
• Previous work indicated that vaccinia intracellular mature virus (IMV) utilizes microtubules to move from the viral factory to the site of intracellular envelopment and that expression of the viral A27 protein is required for this transport [3].
• The polyvalent formulations with various combinations of the four poxvirus antigens (A27, L1, B5 and A33) achieved better protection than the monovalent formulation using only one of these antigens [4].

High impact information on IGKV3-20

• In this paper, a nonrefocused (1)H,(15)N CPMG HSQC of uniformly (13)C,(15)N-labeled 33-mer PEMV-1 RNA has been tailored to reveal a correlation of the 2'-OH hydroxyl proton of C15 to the N1 nitrogen resonance of A27 mediated by a cross hydrogen bond scalar coupling [5].
• A27/80 and OVCAR-3 cells overexpressing H-REV107-1 protein underwent apoptosis [1].
• In the IFNgamma-sensitive cell line A27/80, H-REV107-1 suppresses colony formation [1].
• In comparison, B5- and A27-specific T-cell frequencies ranged from 0.4 to 1.3% in a donor vaccinated 3 years ago [6].
• This interaction mediates a 2.3-A displacement of C8(+) driven by an A27 N6-C8(+) O2 hydrogen bond as part of an A((n-1)).C(+).G-C(n) base quadruple [7].

Biological context of IGKV3-20

• A U23-A27-U38 base triple is proposed based on exchangeable proton NMR data, where U23 forms a base pair with A27 in the major groove [8].
• Overexpression of TIG3 in A27/80 ovarian carcinoma cells significantly impaired cell growth and despite increased mRNA levels, TIG3 protein was hardly detectable [9].
• RESULTS: Subjects homozygous for the most common aggrecan VNTR allele, A27 with 27 repeats, had a significantly lower risk of hand OA, with OR 0.46 (95% CI 0.27-0.78) for OA of grade 2 or more [10].
• In vitro stimulation of eosinophils with cytokines leads to up-regulation of CD11b and priming markers recognized by the recently developed priming markers A17 and A27, whereas interleukin (IL)-5Ralpha is being down-regulated [11].
• An excess of the genotype HL-A27/W10 was found in patients with Reiter's syndrome [12].

Anatomical context of IGKV3-20

• The light (L)-chain V region was of the kappa subgroup III and was 94% identical to the A27 (Humkv325) germ line gene, which is commonly used by rheumatoid factors and other autoantibodies [13].
• The correlation between H(2)O(2) in exhaled air with A27 priming on neutrophils showed that local inflammation has systemic effects on cells of the innate immune system [14].
• Modulation of the leukocyte compartment as a consequence of systemic activation by cytokines/chemokines was determined by measuring the expression of priming-associated epitopes by novel antibodies designated A17 and A27 [14].
• The productive immunoglobulin light chain repertoire in the parotid gland of the SS patient was found to be restricted, showing a preferential usage of particular variable lambda chain genes (V lambda 2E) and variable kappa chain genes (V kappa A27) [15].

Associations of IGKV3-20 with chemical compounds

• Although basal A17 and A27 expression was not increased, we observed a significantly higher expression of these priming epitopes on N-formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated cells of RSV patients compared with cells of controls, indicative of prior in vivo priming [11].

Analytical, diagnostic and therapeutic context of IGKV3-20

• To evaluate VACV-specific memory T-cell responses, peripheral blood mononuclear cells (PBMC) from four VACV vaccinees were tested against whole VACV and the individual envelope proteins A27, B5, L1, and A33, using gamma interferon enzyme-linked immunospot and cytokine flow cytometry assays [6].

References