Decision trees for early prediction of inadequate immune response to coronavirus infections: a pilot study on COVID-19

Introduction: Few artificial intelligence models exist to predict severe forms of COVID-19. Most rely on post-infection laboratory data, hindering early treatment for high-risk individuals. Methods: This study developed a machine learning model to predict inherent risk of severe symptoms after contracting SARS-CoV-2. Using a Decision Tree trained on 153 Alpha variant patients, demographic, clinical and immunogenetic markers were considered. Model performance was assessed on Alpha and Delta variant datasets. Key risk factors included age, gender, absence of KIR2DS2 gene (alone or with HLA-C C1 group alleles), presence of 14-bp polymorphism in HLA-G gene, presence of KIR2DS5 gene, and presence of KIR telomeric region A/A. Results: The model achieved 83.01% accuracy for Alpha variant and 78.57% for Delta variant, with True Positive Rates of 80.82 and 77.78%, and True Negative Rates of 85.00% and 79.17%, respectively. The model showed high sensitivity in identifying individuals at risk. Discussion: The present study demonstrates the potential of AI algorithms, combined with demographic, epidemiologic, and immunogenetic data, in identifying individuals at high risk of severe COVID-19 and facilitating early treatment. Further studies are required for routine clinical integration

Growth and phosphatase activities of ostreopsis cf. Ovata biofilms supplied with diverse dissolved organic phosphorus (DOP) compounds

It is becoming increasingly evident that the use of organic nutrients is widespread among many aquatic phototrophic organisms. Simultaneously, incidents of eutrophication of coastal waters are becoming more common due to rises in organic nutrient loads deriving from anthropogenic activities and natural terrestrial processes. In the northern Adriatic Sea, blooms of the toxic dinoflagellate Ostreopsis cf. ovata are reported as a frequent phenomenon linked to particular environmental conditions, including increased organic nutrient loads. Ostreopsis blooms typically produce a mucilaginous biofilm that can cover all benthic substrata. In order to clarify the role of dissolved organic phosphorus (DOP) in the onset and maintenance of an O. cf. ovata bloom, we investigated the growth rates in the presence of a range of phosphomonoesters (PMEs) (D-fructose 1, 6-disphosphate, β-glycerophosphate, α-D-glucose 1-phosphate, guanosine 5’-monophos-phate and phytic acid) and phosphodiesters (PDEs) (DNA and RNA). Levels of both phosphomonoesterase (PMEase) and phosphodiesterase (PDEase) activities were assessed in the O. cf. ovata biofilms. The results showed that O. cf. ovata growth is not inhibited in media containing a wide range of DOP and diverse ratios of PME:PDE compared to those containing inorganic phosphorus. Much of the hydrolytic activity was associated with bacteria and with extracellular polymeric substances (EPSs). Our findings suggest that the success of O. cf. ovata stems from the collective participation of all components of the biofilm (O. cf. ovata, EPSs and bacteria) that allows it to thrive in phosphorus-limited environments, but where the main source of phosphorus is organic

La pastoral de la comunicación social en torno a Medellín, Puebla y Santo Domingo (1966-1992) : una visión teológica de la búsqueda de un modelo y estilo pastoral para la comunicación solidaria e inculturada del Evangelio en la Iglesia latinoamericana

Al presentar esta disertación a la Pontificia Universidad Católica Argentina Santa María de los Buenos Aires, en la Facultad de Teología, para acceder a la Licenciatura en Sagrada Teología con especialización en Pastoral, indicaremos el ámbito de nuestro estudio. Lo configuraremos en cuatro pasos. El primero abarcará las motivaciones (antropológicas y teológico-pastorales) del tema, luego explicitaremos el objetivo y el fin del mismo. El tercero abordará los criterios orientadores de la investigación para finalizar con la metodología y estructura de la misma

Pre-analytical stability of the plasma proteomes based on the storage temperature

Background: This study examined the effect of storage temperature on the protein profile of human plasma. Plasma samples were stored for 13 days at -80°C, -20°C, +4°C and room temperature (20-25°C) prior to proteomic analysis. The proteomic comparisons were based on the differences of mean intensity values of protein spots between fresh plasma samples (named " time zero" ) and plasma samples stored at different temperatures. To better understand the thermally induced biochemical changes that may affect plasma proteins during storage we identified proteins with different expressions with respect to the time zero sample.Results: Using two-dimensional electrophoresis followed by MALDI-TOF MS and /or LC-MS/MS 20 protein spots representing 10 proteins were identified with significant differences in abundance when stored at different temperatures. Our results, in agreement with various authors, indicate that during storage for a short period (13 days) at four different temperatures plasma proteins were more affected by degradation processes at +4°C compared to the other temperatures analysed. However, we founded that numerous protein spots (vitamin D binding protein, alpha-1-antitrypsin, serotransferrin, apoplipoprotein A-I, apolipoprotein E, haptoglobin and complement factor B) decrease in abundance with increasing temperature up to 4°C, but at room temperature their intensity mean values are similar to those of time zero and -80°C. We hypothesize that these proteins are labile at 4°C, but at the same time they are stable at room temperature (20-25°C). Furthermore we have grouped the proteins based on their different sensitivity to the storage temperature. Spots of serum albumin, fibrinogen gamma chain and haptoglobin are more resistant to the higher temperatures tested, as they have undergone changes in abundance only at room temperature; conversely, other spots of serum albumin, fibrinogen beta chain and serotransferrin are more labile as they have undergone changes in abundance at all temperatures except at -80°C.Conclusions: Although there are many studies concerning protein stability of clinical samples during storage these findings may help to provide a better understanding of the changes of proteins induced by storage temperature