Macacine herpesvirus or B Virus (BV) is a zoonotic agent that leads to high mortality rates in humans if transmitted and untreated. Here, BV is used as a test case to establish a two-step procedure for developing high throughput serological assays based on synthetic peptides. In step 1, peptide microarray analysis of 42 monkey sera (30 of them tested BV positive by ELISA) revealed 1148 responses against 369 different peptides. The latter could be grouped into 142 different antibody target regions (ATRs) in six different glycoproteins (gB, gC, gD, gG, gH, and gL) of BV. The high number of newly detected ATRs was made possible inter alia by a new preanalytical protocol that reduced unspecific binding of serum components to the cellulose-based matrix of the microarray. In step 2, soluble peptides corresponding to eight ATRs of particularly high antigenicity were synthesized and coupled to fluorescently labeled beads, which were subsequently employed in immunochemical bead flow assays. Their outcome mirrored the ELISA results used as reference. Hence, convenient, fast, and economical screening of arbitrarily large macaque colonies for BV infection is now possible. The study demonstrates that a technology platform switch from two-dimensional high-resolution peptide arrays used for epitope discovery to a readily available bead array platform for serology applications is feasible.

A total of 285 children out of an 8 year period with fractures of the forearm were studied. Of these 175 (62.2%) had a fracture of the distal radius and 51 (18.2%) had a fracture of the distal forearm and there were 42 (14.7%) fractures in the middle or proximal third in this region. Three children with injuries of the distal radial epiphysis had to be treated by percutaneous wire fixation. Except for 2 cases who needed surgery all severe dislocated forearm fractures could be treated by closed reduction. In all cases the children were immobilized with a long upper arm cast for 3 to 4 weeks. Follow-up examinations up to 6 years after injury showed excellent results in distal forearm and distal radial fractures whereas results were only satisfactory in midshaft forearm fractures.

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With more than thousand different members that have been discovered yet, zinc finger proteins are considered to be one of the most comprehensive classes of DNA-binding proteins found in nature. [9] This is due to their participation as DNA-binding domains in the modular structure of many eukaryotic and prokaryotic transcription factors. In this function, they are involved in the early steps of DNA transcription, an ubiquitous process that uses the genetic information by translating DNA sequences into corresponding messenger RNAs (mRNAs). Thereby, ZFPs recognize a specific promoter sequence, which is located upstream of the genetic code that should be transcribed by RNA-polymerases (Figure 1.1).Under retention of an uniform globular -structure, zinc fingers differ in their individual amino acid sequences to bind a large variety of promoter regions in a sequence-specific manner. This explains the high diversity of this protein family in the cellular environment and finally allows them to trigger transcriptional processes for a myriad of genes.