PubMed · 8959712
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S J Rodda, N J Maeji, G Tribbick. 1996. Epitope mapping using multipin peptide synthesis.. https://doi.org/10.1385/0-89603-375-9%3A137
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Interactions between inhibitory killer cell immunoglobulin-like receptors (iKIR) and human leukocyte antigen (HLA) class I molecules regulate natural killer (NK) cell responses to eliminate infected and transformed cells while maintaining tolerance to healthy cells. Unlinked polymorphic gene families encode KIR receptors and HLA class I ligands and their independent segregation results in a variable number and type of iKIR + HLA pairs inherited in individuals. The diversity in the co-inheritance of iKIR + HLA pairs and activating KIR (aKIR) genes in 759 unrelated individuals from four ethnic populations was analyzed. Every individual studied inherited a minimum of one iKIR + HLA pair; suggesting that major histocompatibility complex class I-dependent inhibitory KIR signaling is essential for human NK cell function. In contrast, 13.4% of the study group lacked all aKIR genes. Twenty percent of the study group carried only one of the four iKIR + HLA pairs. Interestingly, 3% of the study group carrying only KIR2DL3 + HLA-C1 as an iKIR + HLA pair lacked aKIR genes. These data suggest that a single iKIR can constitute the minimal KIR repertoire for human NK cells. Genotypes carrying an equal number of iKIR + HLA pairs and aKIR genes represented 20% of the study group. The remaining individuals had either a dominant inhibitory KIR genotype (iKIR + HLA > aKIR) or a dominant activating KIR genotype (iKIR + HLA < aKIR). Genotypes encoding these imbalanced inhibitory and activating interactions may contribute to susceptibility or resistance to human diseases.
Molecular imprinting technique is a novel technique based on mimicking specific action of antibody-antigen. The emergence and the development of the technique are reviewed in this article. The focuses of this article include the introductions of the synthesis conditions, the comparisons of the various approaches on preparation methods as well as the recognition mechanisms of the biomacromolecule imprinted polymers. The primary synthetic methods include the embed technique, the surface imprinting procedure and the epitope approach. The epitope approach is based on using a short peptide as a template that represents only part of a larger peptide or protein, which in turn can be recognized by the synthesized polymer. This approach for the development of the biomacromolecule imprinted polymers selective to proteins is attractive from an economic viewpoint: a small peptide is usually less expensive, and the quantity necessary for the polymer preparation is more readily available than that of the corresponding protein. In the end, the limitations and the prospective applications of this biomacromolecular imprinted technique are also discussed.
The growing range of applications for peptide arrays prepared by SPOT synthesis confirms that they are a powerful proteomics technique to study numerous aspects of molecular interaction events. The most frequent application for peptide arrays prepared by SPOT synthesis is the identification of linear epitopes that are recognized by antibodies. In the conventional format using secondary antibodies for detection unspecific binding and high background have been observed. This leads to difficulties in evaluation of developed membranes. Especially for application with combinatorial libraries false positive results are to be avoided. To circumvent this issue, we directly labeled compounds of interest with biotin and detected binding by incubation with streptavidin-horseradish peroxidase via chemiluminescence. Optimization of method conditions led to a very sensitive detection technique with no or low number of unspecific spots, which is superior to conventional detection with secondary antibodies. As one consequence, evaluation of competitive assays got more reliable.