@article{fdi:010077022,
  title = {{I}nhibition of {N}-myristoyltransferase1 affects dengue virus replication},
  author = {{S}uwanmanee, {S}. and {M}ahakhunkijcharoen, {Y}. and {A}mpawong, {S}. and {L}eaungwutiwong, {P}. and {M}iss{\'e}, {D}oroth{\'e}e and {L}uplertlop, {N}.},
  editor = {},
  language = {{ENG}},
  abstract = {{D}engue virus ({DENV}) causes dengue fever, a self-limiting disease that could be fatal due to serious complications. {N}o specific treatment is currently available and the preventative vaccine is only partially protective. {T}o 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. {I}n this study, we investigated the interaction of dengue viral proteins with host {NMT} and its subsequent effect on {DENV}. {O}ur bioinformatics, molecular docking, and far-western blotting analyses demonstrated the interaction of viral envelope protein ({E}) with {NMT}. {T}he gene expression of {NMT} was strongly elevated in a dependent manner during the viral replication phase in dendritic cells. {M}oreover, {NMT} gene silencing significantly inhibited {DENV} replication in dendritic cells. {F}urther studies investigating the target cell types of other host factors are suggested.},
  keywords = {dengue virus ; envelope protein ; {N}-myristoyltransferase1 ; viral replication},
  booktitle = {},
  journal = {{M}icrobiologyopen},
  volume = {8},
  numero = {9},
  pages = {art. e831 [13 ]},
  ISSN = {2045-8827},
  year = {2019},
  DOI = {10.1002/mbo3.831},
  URL = {https://www.documentation.ird.fr/hor/fdi:010077022},
}