Improving readability of patient education materials.

Functional illiteracy contributes to negative long-term health consequences for patients who must understand and adhere to complex health care instructions and, therefore, is of primary importance to community health nurses. This problem is compounded when English is the patient's second language. A process for improving patient education materials (PEMs) through adaptation or creation of new materials to meet the health needs of diverse groups is presented. The process was applied to a popular health education program used with school-age children and their parents to teach them home management of asthma. Target parents were known to read at a 5th-grade level, and English was a second language for many of them. Therefore, extensive revision of the existing PEMs was required. The steps to successful revision included assessing readability and comprehensibility, editing the materials, and evaluating the new PEMs to determine the effectiveness of the revision measures.

Activity of recombinant HIV-1 integrase on mini-HIV DNA.

Integration of the human immunodeficiency virus type 1 (HIV-1) cDNA into the genome of a human cell is an essential step in the viral replication cycle. Understanding of the integration process has been facilitated by the development of in vitro assays using specific oligonucleotides and recombinant integrase. However, understanding of the biology of retroviral integration will require in vitro and in vivo model systems using long DNA substrates that mimic the HIV cDNA. We have now studied the activity of recombinant HIV-1 integrase on a linear 4.7 kb double-stranded DNA, containing flanking regions of approximately 200 bp that represent the intact ends of the HIV-1 long terminal repeat (LTR) sequences (mini-HIV). The strand transfer products of the integration reaction can be directly visualized after separation in agarose gels by ethidium bromide staining. The most prominent reaction product resulted from integration of one LTR end into another LTR end (U5 into U5 and U5 into U3). Sequence analysis of the reaction products showed them to be products of legitimate integration preceded by correct processing of the viral LTR ends. Hotspots for integration were detected. Electron microscopy revealed the presence of a range of reaction products resulting from single or multiple integration events. The binding of HIV-1 integrase to mini-HIV DNA was visualized. Oligomers of integrase seem to induce DNA looping whereby the enzyme often appears to be bound to the DNA substrate that adopts the structure of a three-site synapsis that is reminiscent of the Mu phage transposase complex.