| Gene Name | GARS |
| HF Protein Name | Glycyl-tRNA synthetase |
| HF Function | required for virus infection |
| Uniprot ID | P41250 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 2617 |
| Host Factor (HF) Name in Paper | GARS |
| Gene synonyms | GARS |
| Ensemble Gene ID | ENSG00000106105 |
| Ensemble Transcript | ENST00000389266.8 [P41250-1] |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0004081, GO:0004820, GO:0005524, GO:0005737, GO:0005739, GO:0005759, GO:0005829, GO:0006418, GO:0015966, GO:0030141, GO:0030424, GO:0042802, GO:0046983, GO:0070062, GO:0070150, GO:0141192, |
| MINT ID | P41250 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 600287;600794;601472;619042 |
| PANTHER ID | PTHR10745:SF0;PTHR10745 |
| PDB ID(s) | 2PME, 2PMF, 2Q5H, 2Q5I, 2ZT5, 2ZT6, 2ZT7, 2ZT8, 2ZXF, 4KQE, 4KR2, 4KR3, 4QEI, 5E6M, |
| pfam ID | PF03129, PF00587, PF00458, |
| Drug Bank ID | DB00145, |
| ChEMBL ID | CHEMBL4105815 |
| Organism | Homo sapiens (Human) |
| Virus Name | Nipah Virus |
| Virus Short Name | NiV |
| Order | Mononegavirales |
| Virus Family | Paramyxoviridae |
| Virus Subfamily | N.A. |
| Genus | Henipavirus |
| Species | Nipah henipavirus |
| Host | Vertebrates |
| Cell Tropism | N.A. |
| Associated Disease | Fever and headache |
| Mode of Transmission | Sexual contact, blood, breast feeding |
| VIPR DB link | https://www.viprbrc.org/brc/vipr_search.do?species=Nipah_virus |
| ICTV DB link | https://ictv.global/report/152/paramyxoviridae |
| Virus Host DB link |
| Paper Title | Nipah Virus-Like Particle Egress Is Modulated by Cytoskeletal and Vesicular Trafficking Pathways: a Validated Particle Proteomics Analysis |
| Author's Name | Gunner P. Johnston, Birgit Bradel-Tretheway, Paul D. Piehowski, Heather M. Brewer, Bom Nae Rin Lee, Nicholas T. Usher, J. Lizbeth Reyes Zamora, Victoria Ortega, Erik M. Contreras, Jeremy R. Teuton, Jason P. Wendler, Keesha M. Matz, Joshua N. Adkins, and Hector C. Aguilara |
| Journal Name | mSystems |
| Pubmed ID | 31551400 |
| Abstract | Classified as a biosafety level 4 (BSL4) select agent, Nipah virus (NiV) is a deadly henipavirus in the Paramyxoviridae family, with a nearly 75% mortality rate in humans, underscoring its global and animal health importance. Elucidating the process of viral particle production in host cells is imperative both for targeted drug design and viral particle-based vaccine development. However, little is understood concerning the functions of cellular machinery in paramyxoviral and henipaviral assembly and budding. Recent studies showed evidence for the involvement of multiple NiV proteins in viral particle formation, in contrast to the mechanisms understood for several paramyxoviruses as being reliant on the matrix (M) protein alone. Further, the levels and purposes of cellular factor incorporation into viral particles are largely unexplored for the paramyxoviruses. To better understand the involvement of cellular machinery and the major structural viral fusion (F), attachment (G), and matrix (M) proteins, we performed proteomics analyses on virus-like particles (VLPs) produced from several combinations of these NiV proteins. Our findings indicate that NiV VLPs incorporate vesicular trafficking and actin cytoskeletal factors. The involvement of these biological processes was validated by experiments indicating that the perturbation of key factors in these cellular processes substantially modulated viral particle formation. These effects were most impacted for NiV-F-modulated viral particle formation either autonomously or in combination with other NiV proteins, indicating that NiV-F budding relies heavily on these cellular processes. These findings indicate a significant involvement of the NiV fusion protein, vesicular trafficking, and actin cytoskeletal processes in efficient viral particle formation. |
| Used Model | HEK293T |
| DOI | 10.1128/mSystems.00194-19 |
