Development of a Prehospital Care Rotation for Emergency Medicine Residents in Haiti.

BACKGROUND: Prehospital care is a key component of an emergency care system. Prehospital providers initiate patient care in the field and transition it to the emergency department. Emergency Medicine (EM) specialist training programs are growing rapidly in low- and middle-income countries (LMICs), and future emergency physicians will oversee emergency care systems. Despite this, no standardized prehospital care curriculum exists for physicians in these settings. This report describes the development of a prehospital rotation for an EM residency program in Central Haiti. METHODS: Using a conceptual framework, existing prehospital curricula from high-income countries (HICs) were reviewed and adapted to the Haitian context. Didactics covering prehospital care from LMICs were also reviewed and adapted. Regional stakeholders were identified and engaged in the curriculum development. RESULTS: A one-week long, 40-hour curriculum was developed which included didactic, clinical, evaluation, and assessment components. All senior residents completed the rotation in the first year. Feedback was positive from residents, field sites, and students. CONCLUSIONS: A standardized prehospital rotation for EM residents in Haiti was successfully implemented and well-received. This model of adaptation and local engagement can be applied to other residency programs in low-income countries to increase physician engagement in prehospital care.

Trichoderma reesei cellobiohydrolase II is associated with the outer membrane when overexpressed in Escherichia coli.

Cellulose degradation is essential for the future production of many advanced biofuels. Cellulases from the filamentous fungus Trichoderma reesei are among the most efficient enzymes for the hydrolysis of cellulosic materials. One of the cellulases from T. reesei, cellobiohydrolase II (CBH2), was studied because of its industrial relevance and proven enzymatic activity. Using both crude and rigorous membrane fractionation methods we show that full length T. reesei CBH2 is exclusively localized to the outer membrane when expressed recombinantly in Escherichia coli. Even fusing signal sequence-free maltose-binding protein to the N-terminus of CBH2, which has been shown to increase solubility of other proteins, did not prevent the outer membrane localization of CBH2. These results highlight the difficulties in producing fungal cellulases in bacterial hosts and provide a stepping stone for future cellulase engineering efforts.