Gene Name | HSPA6 |
HF Protein Name | Heat shock 70 kDa protein 6 |
HF Function | Essential for viral replication |
Uniprot ID | Q04967 |
Protein Sequence | View Fasta Sequence |
NCBI Gene ID | 396906 |
Host Factor (HF) Name in Paper | HSP70 |
Gene synonyms | HSP70B |
Ensemble Gene ID | N.A |
Ensemble Transcript | N.A. |
KEGG ID | Go to KEGG Database |
Gene Ontology ID(s) | GO:0005524, |
MINT ID | N.A. |
STRING | Click to see interaction map |
GWAS Analysis | Click to see gwas analysis |
OMIM ID | N.A. |
PANTHER ID | PTHR19375 |
PDB ID(s) | N.A., |
pfam ID | PF00012, |
Drug Bank ID | N.A., |
ChEMBL ID | N.A. |
Organism | Sus scrofa (Pig) |
Virus Name | Porcine reproductive and respiratory syndrome virus |
Virus Short Name | PRRSV |
Order | Nidovirales |
Virus Family | Arteriviridae |
Virus Subfamily | N.A. |
Genus | Porartevirus |
Species | Porcine reproductive and respiratory syndrome virus |
Host | Vertebrates |
Cell Tropism | Primarily it's found in alveolar lung macrophages and macrophages of other tissues, later, is also found in testicular germ cells. |
Associated Disease | Abortions and respiratory disease |
Mode of Transmission | Transplacental, saliva, urine, semen and respiratory tract secretions |
VIPR DB link | N.A. |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/220/arteriviridae |
Virus Host DB link | N.A. |
Paper Title | Inhibition of HSP70 reduces porcine reproductive and respiratory syndrome virus replication in vitro |
Author's Name | Gao J, Xiao S, Liu X, Wang L, Ji Q, Mo D, Chen Y |
Journal Name | BMC Microbiolog |
Pubmed ID | 24625230 |
Abstract | BACKGROUND Successful viral infection requires the involvement of host cellular factors in their life cycle. Heat shock protein 70 (HSP70) can be recruited by numerous viruses to promote the folding, maturation, or assembly of viral proteins. We have previously shown that HSP70 is significantly elevated in porcine reproductive and respiratory syndrome virus (PRRSV)-infected lungs, suggesting HSP70 may play a potential role during PRRSV infection. In this study, we tried to investigate the role of HSP70 during PRRSV infection. RESULTS In this study, we observed that PRRSV infection induced the expression of HSP70. The down-regulation of HSP70 using quercetin, a HSPs synthesis inhibitor, or small interfering RNAs (siRNA) reduced the viral protein level and viral production. Notably, these inhibitory effects on PRRSV infection could be attenuated by heat shock treatment. In addition, HSP70 was found to colocalize with the viral double-stranded RNA (dsRNA) and knockdown of HSP70 decreased the dsRNA levels, suggesting HSP70 is involved in the formation of viral replication and transcription complex (RTC) and thus affects the viral replication. CONCLUSIONS Our study revealed that HSP70 is an essential host factor required for the replication of PRRSV. The inhibition of HSP70 significantly reduced PRRSV replication, which may be applied as an effective antiviral strategy. |
Used Model | MARC 145 cells |
DOI | 10.1186/1471-2180-14-64 |