RESUMO
Dengue virus (DENV) causes dengue fever, a self-limiting disease that could be fatal due to serious complications. No specific treatment is currently available and the preventative vaccine is only partially protective. To develop a potential drug target for dengue fever, we need to understand its biology and pathogenesis thoroughly. N-myristoyltransferase (NMT) is an N-terminal protein lipidation enzyme that catalyzes the covalent cotranslational attachment of fatty acids to the amino-terminal glycine residue of a number of proteins, leading to the modulation of various signaling molecules. In this study, we investigated the interaction of dengue viral proteins with host NMT and its subsequent effect on DENV. Our bioinformatics, molecular docking, and far-western blotting analyses demonstrated the interaction of viral envelope protein (E) with NMT. The gene expression of NMT was strongly elevated in a dependent manner during the viral replication phase in dendritic cells. Moreover, NMT gene silencing significantly inhibited DENV replication in dendritic cells. Further studies investigating the target cell types of other host factors are suggested.
Assuntos
Aciltransferases/metabolismo , Vírus da Dengue/crescimento & desenvolvimento , Interações Hospedeiro-Patógeno , Proteínas do Envelope Viral/metabolismo , Replicação Viral , Aciltransferases/antagonistas & inibidores , Aciltransferases/genética , Células Cultivadas , Células Dendríticas/virologia , Técnicas de Silenciamento de Genes , Humanos , Mapeamento de Interação de ProteínasRESUMO
In an evaluation of the API 20NE for the identification of Burkholderia spp., 792/800 (99%) Burkholderia pseudomallei and 17/19 (89%) B. cepacia isolates were correctly identified but 10 B. mallei and 98 B. thailandensis isolates were not correctly identified. A latex agglutination test was positive for 796/800 (99.5%) B. pseudomallei isolates and negative for 120 other oxidase-positive gram-negative bacilli.