Transformation of World Health Organization's management practice and workforce to fit the priorities of African countries.

INTRODUCTION: The WHO Regional Office for Africa developed an evidence-based tool, called the Dalberg tool to guide the functional review and restructuring of the workforce and management of the country offices to better fit the health priorities of Member States. METHODS: The Dalberg tool was used in conjunction with a series of consultations and dialogues to review twenty-two countries have undergone the functional review. Results: the "core functions" in WHO country offices (WCOs) were identified. These are health coordination, strengthening of health systems, generation of evidence and strategic information management, and preparedness against health emergencies. RESULTS: In order to standardize country office functions, categorization of countries was undertaken, based on specific criteria, such as health system performance towards Universal Health Coverage (UHC), health emergencies, burden of communicable and non-communicable diseases, subnational presence and national population size. CONCLUSION: Following the functional review, the staff is now better aligned with country and organizational priorities. For example, the functional review has taken into consideration: (i) the ongoing polio transition planning; (ii) the implementation of the WHO emergency programme in countries; (iii) the investment case for strengthening routine immunization in Africa; and (iv) regional flagship programmes, such as adolescent health and UHC. The delivery of the core functions above will require the hiring of additional capacities and expertise in most country offices if deemed fit-for-purpose.

Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures.

Prion rods, i.e. insoluble infectious aggregates of the N-terminally truncated form of the prion protein, PrP 27-30, and the corresponding recombinant protein, rPrP(90-231), were autoclaved in water, bovine lipid or lipid-water mixtures for 20 min at temperatures from 100 to 170 degrees C. A protocol was developed for the quantitative precipitation of small amounts of protein from large excesses of lipid. PrP remaining undegraded after autoclaving was quantified by Western blot and degradation factors were calculated. The Arrhenius plot of the rate of degradation vs temperature yielded linear relationships for prion rods in water or lipid-water as well as for rPrP(90-231) in lipid-water. The presence of lipids increased the heat stability of prion rods, especially at lower temperatures. Prion rods had a much higher thermal stability compared to rPrP. Autoclaving of prion rods in pure lipid gave different results - not simple degradation but bands indicative of covalently linked dimers, tetramers and higher aggregates. The heat stability of prion rods in pure lipid exceeded that in lipid-water mixtures. Degradation factors larger than 10(4) were reached at 170 degrees C in the presence of lipids and at 150 degrees C in the absence of lipids. The linear correlation of the data allows cautious extrapolation to conditions not tested, i.e. temperatures higher than 170 degrees C. A factual basis for assessing the biological safety of industrial processes utilizing potentially BSE-or scrapie-contaminated animal fat is provided.