Inhibition of N‐myristoyltransferase1 affects dengue virus replication
Abstract 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 understa...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2019-09-01
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| Series: | MicrobiologyOpen |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/mbo3.831 |
| _version_ | 1819115205086412800 |
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| author | San Suwanmanee Yuvadee Mahakhunkijcharoen Sumate Ampawong Pornsawan Leaungwutiwong Dorothée Missé Natthanej Luplertlop |
| author_facet | San Suwanmanee Yuvadee Mahakhunkijcharoen Sumate Ampawong Pornsawan Leaungwutiwong Dorothée Missé Natthanej Luplertlop |
| author_sort | San Suwanmanee |
| collection | DOAJ |
| description | Abstract 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. |
| first_indexed | 2024-12-22T04:57:29Z |
| format | Article |
| id | doaj.art-938011b9c7e74d9484a8d01fb880a334 |
| institution | Directory Open Access Journal |
| issn | 2045-8827 |
| language | English |
| last_indexed | 2024-12-22T04:57:29Z |
| publishDate | 2019-09-01 |
| publisher | Wiley |
| record_format | Article |
| series | MicrobiologyOpen |
| spelling | doaj.art-938011b9c7e74d9484a8d01fb880a3342022-12-21T18:38:21ZengWileyMicrobiologyOpen2045-88272019-09-0189n/an/a10.1002/mbo3.831Inhibition of N‐myristoyltransferase1 affects dengue virus replicationSan Suwanmanee0Yuvadee Mahakhunkijcharoen1Sumate Ampawong2Pornsawan Leaungwutiwong3Dorothée Missé4Natthanej Luplertlop5Department of Microbiology and Immunology Faculty of Tropical Medicine Mahidol University Bangkok ThailandDepartment of Microbiology and Immunology Faculty of Tropical Medicine Mahidol University Bangkok ThailandDepartment of Tropical Pathology Faculty of Tropical Medicine Mahidol University Bangkok ThailandDepartment of Microbiology and Immunology Faculty of Tropical Medicine Mahidol University Bangkok ThailandMIVEGEC UMR 224, Université de Montpellier, IRD, CNRS Montpellier FranceDepartment of Microbiology and Immunology Faculty of Tropical Medicine Mahidol University Bangkok ThailandAbstract 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.https://doi.org/10.1002/mbo3.831dengue virusenvelope proteinN‐myristoyltransferase1viral replication |
| spellingShingle | San Suwanmanee Yuvadee Mahakhunkijcharoen Sumate Ampawong Pornsawan Leaungwutiwong Dorothée Missé Natthanej Luplertlop Inhibition of N‐myristoyltransferase1 affects dengue virus replication MicrobiologyOpen dengue virus envelope protein N‐myristoyltransferase1 viral replication |
| title | Inhibition of N‐myristoyltransferase1 affects dengue virus replication |
| title_full | Inhibition of N‐myristoyltransferase1 affects dengue virus replication |
| title_fullStr | Inhibition of N‐myristoyltransferase1 affects dengue virus replication |
| title_full_unstemmed | Inhibition of N‐myristoyltransferase1 affects dengue virus replication |
| title_short | Inhibition of N‐myristoyltransferase1 affects dengue virus replication |
| title_sort | inhibition of n myristoyltransferase1 affects dengue virus replication |
| topic | dengue virus envelope protein N‐myristoyltransferase1 viral replication |
| url | https://doi.org/10.1002/mbo3.831 |
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