| Gene Name | BAG3 |
| HF Protein Name | BAG family molecular chaperone regulator 3 |
| HF Function | Antiviral protein |
| Uniprot ID | O95817 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 9531 |
| Host Factor (HF) Name in Paper | BAG3 |
| Gene synonyms | BIS |
| Ensemble Gene ID | ENSG00000151929 |
| Ensemble Transcript | ENST00000369085 |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0000774, GO:0005634, GO:0005737, GO:0005829, GO:0005886, GO:0006457, GO:0007420, GO:0008625, GO:0010664, GO:0021510, GO:0030018, GO:0034605, GO:0042993, GO:0043005, GO:0043066, GO:0045296, GO:0046827, GO:0050821, GO:0051087, GO:0071260, GO:0097192, GO:0097201, GO:1900034, |
| MINT ID | O95817 |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | 603883 |
| PANTHER ID | N.A. |
| PDB ID(s) | N.A., |
| pfam ID | PF02179, PF00397, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Homo sapiens (Human) |
| Virus Name | Zaire ebolavirus |
| Virus Short Name | ZEBOV |
| Order | Bunyavirales |
| Virus Family | Filoviridae |
| Virus Subfamily | N.A. |
| Genus | Ebolavirus |
| Species | Zaire ebolavirus |
| Host | Bats, human and primates |
| Cell Tropism | N.A. |
| Associated Disease | Hemorragic fever |
| Mode of Transmission | Zoonosis, contact with body fluids |
| VIPR DB link | http://www.viprbrc.org/brc/vipr_allSpecies_search.do?method=SubmitForm&decorator=filo |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/197/filoviridae |
| Virus Host DB link | N.A. |
| Paper Title | Chaperone Mediated Autophagy Protein BAG3 Negatively Regulates Ebola and Marburg VP40 Mediated Egress |
| Author's Name | Jingjing Liang, Cari A. Sagum, Mark T. Bedford, Sachdev S. Sidhu, Marius Sudol, Ziying Han, Ronald N. Harty |
| Journal Name | PLOS Pathogens |
| Pubmed ID | 28076420 |
| Abstract | Ebola (EBOV) and Marburg (MARV) viruses are members of the Filoviridae family which cause outbreaks of hemorrhagic fever. The filovirus VP40 matrix protein is essential for virus assembly and budding, and its PPxY L-domain motif interacts with WW-domains of specific host proteins, such as Nedd4 and ITCH, to facilitate the late stage of virus-cell separation. To identify additional WW-domain-bearing host proteins that interact with VP40, we used an EBOV PPxY-containing peptide to screen an array of 115 mammalian WW-domain-bearing proteins. Using this unbiased approach, we identified BCL2 Associated Athanogene 3 (BAG3), a member of the BAG family of molecular chaperone proteins, as a specific VP40 PPxY interactor. Here, we demonstrate that the WW-domain of BAG3 interacts with the PPxY motif of both EBOV and MARV VP40 and, unexpectedly, inhibits budding of both eVP40 and mVP40 virus-like particles (VLPs), as well as infectious VSV-EBOV recombinants. BAG3 is a stress induced protein that regulates cellular protein homeostasis and cell survival through chaperone-mediated autophagy (CMA). Interestingly, our results show that BAG3 alters the intracellular localization of VP40 by sequestering VP40 away from the plasma membrane. As BAG3 is the first WW-domain interactor identified that negatively regulates budding of VP40 VLPs and infectious virus, we propose that the chaperone-mediated autophagy function of BAG3 represents a specific host defense strategy to counteract the function of VP40 in promoting efficient egress and spread of virus particles. |
| Used Model | HEK293T, HeLa, BHK cells |
| DOI | 10.1371/journal.ppat.1006132 |
