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Allergy poses a heavy health burden in modern society. Other than symptom-relieving medications, the only available treatment approach is allergen-specific immunotherapy, which in spite of offering a potential cure, requires a long treatment duration with multiple doses of allergen administration and carries a risk of anaphylaxis. Gene therapy has shown advantages in experimental studies for treatment of tumors, genetic diseases, chronic infections, and allergy. To date, adenovirus has been the most extensively used gene transfer vector, and offers high efficiency and safety. Here, we review studies of adenovirus-mediated gene therapy targeting different steps in the development of allergic diseases. Adenovirus-mediated gene therapy might be a promising add-on therapy for allergy treatment. [ABSTRACT FROM AUTHOR]

Little is known about pollen-food allergy syndrome (PFS) in China. To investigate the clinical characteristics, as well as sensitization patterns, of PFS in China. Clinical parameters and serum Immunoglobulin E (IgE) responses to prevalent pollens, plant foods and corresponding allergen components were evaluated. The top three most common pollen-associated allergenic foods were peach, apple and pear. Fifty-nine percent of the patients with PFS were allergic to peach. Sixty-one percent of PFS patients developed systemic reactions with or without oral cavity discomfort upon ingestion of the culprit food. Positive IgE responses to nonspecific lipid transfer proteins occurred in 69.9% of PFS patients, which was in accordance with the high prevalence of systemic reactions. Peach was the most common allergenic food in PFS patients. Patients with PFS in China showed an LTP-dominant sensitization profile and usually presented systemic reactions upon consumption of the allergenic foods. [ABSTRACT FROM AUTHOR]

Presents information on a study which analyzed the crystal structure of hydroquinone-beta-cyclodextrin (CD) complex. Discussion on supramolecular chemistry; Synthesis of beta-CD and hydroquinone inclusion complex; Measurements of crystal structure; Results and discussion.

Objective To prokaryotically express mouse stimulated by retinoic acid gene 8 (Stra8) and prepare rabbit anti-mouse Stra8 polyclonal antibody. Methods The recombinant plasmid pET28a-Stra8 was constructed by cloning technology and identified by double enzyme digestion and sequencing, and then transformed into E. coli BL21 (DE3). The expression of Stra8 recombinant protein was induced by IPTG. The prokaryotic protein was purified by His-TAG affinity chromatograph and then used to immune New Zealand white rabbits to obtain Stra8 polyclonal antibody. ELISA, Western blot and immunofluorescence assays were used to determine the antibody titer, validity and specificity, respectively. Results The recombinant plasmid pET28a-Stra8 was constructed successfully as double enzyme digestion and sequencing showed, and the prokaryotic protein was expressed and purified effectively. The titer of the polyclonal antibody reached 1:10 6 . Western blotting showed that the polyclonal antibody could specifically recognize native Stra8 protein in the testis. Immunofluorescence assay revealed that the polyclonal antibody had good reactivity, and could recognize Stra8 protein in mouse testis. Conclusion Stra8 prokaryotic protein can be effectively induced in E. coli and specific rabbit anti-Stra8 polyclonal antibody has been prepared.

Protein inhibitor of activated signal transducer and activator of transcription 2 (PIAS2) is a member of the PIAS protein family. This protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. To improve understanding of the physiological roles of PIAS2, the current study used a yeast two‑hybrid system to screen mouse stem cell cDNA libraries for proteins that interact with PIAS2. The screening identified an interaction between PIAS2 and ubiquitously expressed transcript (UXT). UXT, also termed androgen receptor trapped clone‑27, is an α‑class prefoldin‑type chaperone that acts as a coregulator for various transcription factors, including nuclear factor‑κB and androgen receptor (AR). A direct interaction between PIAS2 and UXT was confirmed by direct yeast two‑hybrid analysis. In vitro evidence of the association of UXT with PIAS2 was obtained by co‑immunoprecipitation. Colocalization between PIAS2 and UXT was identified in the nucleus and cytoplasm of HEK 293T and human cervical carcinoma HeLa cells. The results of the current study suggested that UXT is a binding protein of PIAS2, and interaction between PIAS2 and UXT may be important for the transcriptional activation of AR.