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Since Brazil's major energy resources are renewable and directly related to climate factors, it is among the countries most likely of being affected by climate change. Given Brazil's high hydropower storage capacity and the strong seasonal patterns of its renewable resources, introducing Seasonal Pumped Hydropower Storage (SPHS) can help mitigate these challenges. To this end, a methodology is proposed that links the dynamic system-optimization model – MESSAGEix - to regional climate model simulations, called the Brazilian Electricity System MESSAGEix Model (BESMM). This model, with its detailed hydropower representation, is capable of integrating data from three climate change scenarios with the country's energy system. Climate change introduces a new dimension to this approach, as there is evidence of increasing the seasonal imbalance of variable renewable resources in Brazil. BESMM results suggest that SPHS can play a fundamental role in achieving a 100 % renewable matrix by 2100 in RCP 2.6 scenario, as well as enhancing the renewable energy endowment in scenarios RCP 4.5 and RCP 8.5. A reduction of up to 68 % of CO2emissions is predicted in scenarios incorporating SPHS, compared to scenarios without SPHS.

Rhinoviruses (RVs) are the pathogens most often responsible for the common cold, and are a frequent cause of exacerbations in asthma, chronic obstructive pulmonary disease and cystic fibrosis. Here we report the discovery of IMP-1088, a picomolar dual inhibitor of the human N-myristoyltransferases NMT1 and NMT2, and use it to demonstrate that pharmacological inhibition of host-cell N-myristoylation rapidly and completely prevents rhinoviral replication without inducing cytotoxicity. The identification of cooperative binding between weak-binding fragments led to rapid inhibitor optimization through fragment reconstruction, structure-guided fragment linking and conformational control over linker geometry. We show that inhibition of the co-translational myristoylation of a specific virus-encoded protein (VP0) by IMP-1088 potently blocks a key step in viral capsid assembly, to deliver a low nanomolar antiviral activity against multiple RV strains, poliovirus and foot and-mouth disease virus, and protection of cells against virus-induced killing, highlighting the potential of host myristoylation as a drug target in picornaviral infections. An effective antiviral against the common cold could prevent exacerbations in asthma and chronic obstructive pulmonary disease, but the diversity and adaptability of the virus makes it a highly challenging target. Now, picomolar inhibitors of a human lipid transferase have been developed. Targeting this human lipid transferase could provide an effective and broad-spectrum approach to block viral replication in the host.

Diagnostic tests for foot-and-mouth disease (FMD) include the detection of antibodies against either the viral nonstructural proteins or the capsid. The detection of antibodies against the structural proteins (SP) of the capsid can be used to monitor seroconversion in both infected and vaccinated animals. However, SP tests need to be tailored to the individual FMD virus (FMDV) serotype and their sensitivity may be affected by antigenic variability within each serotype and mismatching between test reagents.