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Projeto de investigação
Lipid-tagged peptides as entry inhibitors for respiratory viruses
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UV-C irradiation-based inactivation of SARS-CoV-2 in contaminated porous and non-porous surfaces
Publication . Tomás, Ana Luísa; Reichel, Anna; Silva, Patrícia M.; Silva, Pedro G.; Pinto, João; Calado, Inês; Campos, Joana; Silva, Ilídio; Machado, Vasco; Laranjeira, Roberto; Abreu, Paulo; Mendes, Paulo; Sedrine, Nabiha Ben; Santos, Nuno C.
The SARS-CoV-2 pandemic emphasized effective cleaning and disinfection of common spaces as an essential tool to mitigate viral transmission. To address this problem, decontamination technologies based on UV-C light are being used. Our aim was to generate coherent and translational datasets of effective UV-C-based SARS-CoV-2 inactivation protocols for the application on surfaces with different compositions. Virus infectivity after UV-C exposure of several porous (bed linen, various types of upholstery, synthetic leather, clothing) and non-porous (types of plastic, stainless steel, glass, ceramics, wood, vinyl) materials was assessed through plaque assay using a SARS-CoV-2 clinical isolate. Studies were conducted under controlled environmental conditions with a 254-nm UV-C lamp and irradiance values quantified using a 254 nm-calibrated sensor. From each material type (porous/non-porous), a product was selected as a reference to assess the decrease of infectious virus particles as a function of UV-C dose, before testing the remaining surfaces with selected critical doses. Our data show that UV-C irradiation is effectively inactivating SARS-CoV-2 on both material types. However, an efficient reduction in the number of infectious viral particles was achieved much faster and at lower doses on non-porous surfaces. The treatment effectiveness on porous surfaces was demonstrated to be highly variable and composition-dependent. Our findings will support the optimization of UV-C-based technologies, enabling the adoption of effective customizable protocols that will help to ensure higher antiviral efficiencies.
The importance of lipid conjugation on anti-fusion peptides against Nipah virus
Publication . Marques, Marta C.; Lousa, Diana; Silva, Patrícia M.; Faustino, André F.; Soares, Cláudio M.; Santos, Nuno C.
Nipah virus (NiV) is a recently emerging zoonotic virus that belongs to the Paramyxoviridae family and the Henipavirus genus. It causes a range of conditions, from asymptomatic infection to acute respiratory illness and fatal encephalitis. The high mortality rate of 40 to 90% ranks these viruses among the deadliest viruses known to infect humans. Currently, there is no antiviral drug available for Nipah virus disease and treatment is only supportive. Thus, there is an urgent demand for efficient antiviral therapies. NiV F protein, which catalyzes fusion between the viral and host membranes, is a potential target for antiviral drugs, as it is a key protein in the initial stages of infection. Fusion inhibitor peptides derived from the HRC-domain of the F protein are known to bind to their complementary domain in the protein's transient intermediate state, preventing the formation of a six-helix bundle (6HB) thought to be responsible for driving the fusion of the viral and cell membranes. Here, we evaluated the biophysical and structural properties of four different C-terminal lipid-tagged peptides. Different compositions of the lipid tags were tested to search for properties that might promote efficacy and broad-spectrum activity. Fluorescence spectroscopy was used to study the interaction of the peptides with biomembrane model systems and human blood cells. In order to understand the structural properties of the peptides, circular dichroism measurements and molecular dynamics simulations were performed. Our results indicate a peptide preference for cholesterol-enriched membranes and a lipid conjugation-driven stabilization of the peptide α-helical secondary structure. This work may contribute for the development of highly effective viral fusion against NiV inhibitors.
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Entidade financiadora
Fundação para a Ciência e a Tecnologia
Programa de financiamento
OE
Número da atribuição
SFRH/BD/118413/2016