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Resumen Introducción: Sarocladium kiliense es un hongo saprófito que puede generar infecciones oportunistas asociadas a procedimientos invasores. Se informa un brote multicéntrico nosocomial de fungemias de fuente común por este agente. Luego del reporte de cinco casos en pacientes en tres hospitales al Programa de Control de Infecciones del Ministerio de Salud de Chile en julio de 2013, se estudiaron a nivel nacional todos los pacientes con hemocultivo positivo para este agente. Se trató de cuadros clínicos leves a moderados, sin muertes atribuibles. El estudio identificó 65 casos en 8 hospitales, en su mayoría pacientes pediátricos en quimioterapia. Estudios iniciales de 94 muestras de cuatro fármacos y dispositivos usados en todos los casos resultaron negativas hasta que, en un segundo análisis de lotes seleccionados por criterios epidemiológicos y su matriz farmacéutica, se identificó la contaminación intrínseca de ampollas de ondansetrón de un productor específico, que se usó en todos los casos. Se realizó un retiro nacional de las ampollas de los tres lotes contaminados del fármaco, después de lo cual se contuvo el brote. La vigilancia de infecciones en los hospitales y el programa nacional coordinado con los laboratorios de microbiología fueron claves para identificar un brote multicéntrico de fuente común por contaminación de un fármaco por un hongo inusual. Sarocladium kiliense is a saprophyte fungus that can cause opportunistic infections associated to invasive procedures. We report a multi-hospital nosocomial outbreak of fungemias due to this agent. Patients with positive blood culture to this agent were studied after six bloodstream infections identified in three Chilean hospitals in July 2013 were reported to Ministry of Health National Infection and Prevention Control Program. In general, there were mild clinical manifestations, without deaths attributable to the infection. Epidemiological and micro-biological study identified 65 cases in 8 hospitals, mostly pediatric patients in chemotherapy. Initial studies of 94 different drugs and medical devices had negative results, until a second analysis of specific blisters and their pharmaceutical matrix selected by epidemiological criteria identified an intrinsic contamination of ondansetron blisters from a specific producer used in all the patients. A recall of contaminated ondansetron blisters was performed in all the country, after which the outbreak was contained. Surveillance and response of local and national infection prevention and control programs and laboratory support were key to control of a national multi-hospital common source outbreak due to contamination of a drug by an unusual fungus.

Resumen del póster presentado al XXXVII Congreso de la Sociedad Española de Bioquímica y Biología Molecular, celebrado en Granada del 9 al 12 de septiembre de 2014., Calmodulin (CaM) is a Ca2+-receptor protein that regulates more than one hundred target proteins with and without enzymatic activity in Ca2+- dependent and independent manners and modulates a myriad of cellular processes, some of which are vital for tumorigenesis (i.e. cell proliferation, apoptosis and autophagy). c-Src is a non-receptor tyrosine kinase that participates in signaling pathways that transduces events initiated by different types of cellular receptors and adhesion molecules, and controls many cellular functions including: cell migration, proliferation, differentiation, apoptosis and stress-response, among others. It has been previously demonstrated that CaM directly interacts with c-Src in a partial Ca2+-dependent manner and that trifl uoperazine, a CaM antagonist, inhibits the phosphorylation of c-Src, suggesting that CaM plays an important role in survival signals in pancreatic tumor cells. We demonstrate in this work that recombinant c-Src directly binds CaM in Ca2+-dependent and independent manners, suggesting that this kinase likely has more than one CaM-binding domain. A couple of IQ-like motifs identified in silico in c-Src could be responsible for the binding of CaM to this kinase in the absence of Ca2+. We also show that CaM enhances the autophosphorylation and tyrosine kinase activity of c-Src in the absence and presence of Ca2+, most strongly in the former condition. We are testing whether the CaM antagonist W-7 inhibits or not the hydrogen peroxideinduced phosphorylation of c-Src in human breast adenocarcinoma SKBR-3 cells, and whether or not CaM-dependent protein kinase II and/or the CaM-regulated protein phosphatase calcineurin, play a role in this process., Funded by SAF2011-23494, S2011/BMD-2349 and PITN-GA-2011-289033 to AV.