No abstract available.
Antibodies, Monoclonal* ; Brain* ; Epitopes* ; Humans*

Epitopes, T-Lymphocyte* ; Poliovirus* ; T-Lymphocytes*

Hyaluronic acid fillers have been proposed as an alternative to other temporary skin fillers for treating facial skin lines and providing soft tissue augmentation. There is no antigenic specificity for species or tissue; thus, these agents have a low potential for allergic or immunogenic reaction. However, there are a few reports about allergic hypersensitivity reactions to hyaluronic acid. We report here on the case of a woman who developed a delayed hypersensitivity reaction to the non-animal stabilized hyaluronic acid filler, Restylane(R).
Epitopes ; Female ; Humans ; Hyaluronic Acid ; Hypersensitivity ; Hypersensitivity, Delayed ; Skin

BACKGROUND: Multiple alloimmunization is the production of two or more alloantibodies by an individual. These antibodies are significant because they can present major problems in compatibility testing. The goal of this study was to determine the properties of concurrent blood group (BG) antibodies in Korea. METHODS: The transfusion records of 540 patients from Dong-A University Hospital were reviewed to identify alloimmunized individuals. The records spanned a time period from September 2002 to March 2010. The data regarding transfusions and the clinical characteristics of those patients making concurrent antibodies were gathered. RESULTS: Concurrent blood group antibodies were found in 23.9% (45/188) of alloimmunized patients, constituting 40.7% (100/246) of all antibodies. The most common alloantibody pair were anti-E/-c and anti-C/-e. The mean transfused RBC units, mean interval, and mean transfusion frequencies before detection of two or more antibodies were 2.4 units, 92 days, and 2.4 times, respectively. The majority of alloantibody pairs appeared and were undetectable at the same time. Among 45 patients (mean age 55.9 years, range 32 to 82 years), twenty-six (57.8%) were female and the remaining nineteen were male. Non-hematological malignancy accounted for a major share (26.7%) in the underlying disease. CONCLUSION: Antibody concurrence varied by BG antigenic specificity. Rh antibodies, in particular anti-E with anti-c appeared to be highly linked. Unlike in Western countries, anti-K was less common in Korea and so the pairs involving this antibody were scarce. More prospective investigations are needed to delineate the immunologic phenomenon of multiple alloimmunization.
Antibodies ; Epitopes ; Female ; Humans ; Isoantibodies ; Korea ; Male ; Mass Screening

G-protein–coupled receptors (GPCRs) are one of the most attractive therapeutic target classes because of their critical roles in intracellular signaling and their clinical relevance to a variety of diseases, including cancer, infection and inflammation. However, high conformational variability, the small exposed area of extracellular epitopes and difficulty in the preparation of GPCR antigens have delayed both the isolation of therapeutic anti-GPCR antibodies as well as studies on the structure, function and biochemical mechanisms of GPCRs. To overcome the challenges in generating highly specific anti-GPCR antibodies with enhanced efficacy and safety, various forms of antigens have been successfully designed and employed for screening with newly emerged systems based on laboratory animal immunization and high-throughput-directed evolution.
Animals, Laboratory ; Antibodies* ; Epitopes ; Immunization ; Inflammation ; Mass Screening

The pattern of DNCB (2, 4-dinitrochlorobenzene) oral desensitization and its antigenic specificity were investigated in guinea pigs. In search of antigenic specificity of DNCB oral desensitization, animals were fed oxazolone (4-ethoxymethylene-2- phenyl-oxazol-5-one) in a DNCB presensitized group, and conversely, DNCB fed in an oxazolone presensitized group. For the study of the pattern of oral desensitization, guinea pigs were initially sensitized to DNCB and followed by feeding of DNCB for 6 days, and challenged on the 13th, 21st, 29th, 37th and 45th days after sensitization. Oxazolone feeding in DNCB presensitized guinea pigs had no effect on the development of the fully responsive DNCB contact sensitivity (72. 85g), and DNCB feeding in oxazolone pre-primed animal had no effect on the development of oxazolone contact sensitivity (79. 37g). On the contrary, oxazolone feeding in DNCB preprimed guinea pigs and DNCB feeding in oxazolone pre-primed resulted in, respectively, oxazolone and DNCB oral tolerance (44.44% p < 0.01 & 42.06%p<0.01). The effect of desensitization appeared even one day before the completion of 6 days' feeding and the efficacy lasted about 30 days by the natural waning of contact sensitivity.
Animals ; Dermatitis, Contact ; Dinitrochlorobenzene* ; Epitopes ; Guinea Pigs* ; Guinea* ; Oxazolone

Epitopes ; immunology ; Hepacivirus ; immunology ; Hepatitis C ; immunology ; Humans

Animals ; Biomarkers ; metabolism ; Epitopes ; metabolism ; Humans ; Immunohistochemistry ; Sweat Glands ; metabolism

We designed a weighted cross-correlation coefficient considering the "anchor" of the T cell epitopes, and used an evolutionary algorithm to search for an optimal weight vector. A SVM model with this new peptide similarity kernel was evaluated on a T-cell data set. The results demonstrated a good performance of this method.
Algorithms ; Artificial Intelligence ; Epitopes, T-Lymphocyte ; Models, Statistical ; Peptides

To establish a method for identifying protein epitopes recognized by therapeutic monoclonal antibodies, the programmed death receptor-1 (PD-1) was selected as the target protein. Based on the alanine scanning strategy, a rapid expression method of antigen mutants combining site-directed mutagenesis with mammalian cell expression system was established, the conditions for eukaryotic expression element amplification and cell transfection expression were established. 150 PD-1 protein mutants were co-expressed, and the binding ability of these mutants to anti-PD-1 antibody Pembrolizumab was identified. The epitopes of Pembrolizumab were determined based on the binding ability of protein mutants to antibodies and combined with protein structure analysis, which was highly consistent with the reported crystal structure-based epitopes, indicating that this method is simple and accurate and can be used for epitope mapping of therapeutic monoclonal antibodies.
Animals ; Antibodies, Monoclonal ; Antigens ; Epitope Mapping ; Epitopes/genetics*