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- Publisher Website: 10.1021/acsinfecdis.6b00064
- Scopus: eid_2-s2.0-84991523589
- PMID: 27626099
- WOS: WOS:000379638600005
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Article: Peptide-Mediated Interference of PB2-eIF4G1 Interaction Inhibits Influenza A Viruses’ Replication in Vitro and in Vivo
Title | Peptide-Mediated Interference of PB2-eIF4G1 Interaction Inhibits Influenza A Viruses’ Replication in Vitro and in Vivo |
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Authors | |
Keywords | Influenza virus Antiviral peptide Host−virus interaction eIF4G1 PB2 Tat |
Issue Date | 2016 |
Publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/aidcbc |
Citation | ACS Infectious Diseases, 2016, v. 2 n. 7, p. 471-477 How to Cite? |
Abstract | Influenza viruses are obligate parasites that hijack the host cellular system. Previous results have shown that the influenza virus PB2 subunit confers a dependence of host eukaryotic translation initiation factor 4-γ 1 (eIF4G1) for viral mRNA translation. Here, we demonstrated that peptide-mediated interference of the PB2-eIF4G1 interaction inhibited virus replication in vitro and in vivo. Remarkably, intranasal administration of the peptide provided 100% protection against lethal challenges of influenza A viruses in BALB/c mice, including H1N1, H5N1, and H7N9 influenza virus subtypes. Mapping of the PB2 protein indicated that the eIF4G1 binding sites resided within the PB2 cap-binding domain. Virtual docking analysis suggested that the inhibitory peptide associated with the conserved amino acid residues that were essential to PB2 cap-binding activity. Overall, our results identified the PB2-eIF4G1 interactive site as a druggable target for influenza therapeutics. |
Persistent Identifier | http://hdl.handle.net/10722/232879 |
ISSN | 2023 Impact Factor: 4.0 2023 SCImago Journal Rankings: 1.179 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yuan, S | - |
dc.contributor.author | Chu, H | - |
dc.contributor.author | Ye, J | - |
dc.contributor.author | Hu, M | - |
dc.contributor.author | Singh, K | - |
dc.contributor.author | Chow, BKC | - |
dc.contributor.author | Zhou, J | - |
dc.contributor.author | Zheng, B | - |
dc.date.accessioned | 2016-09-20T05:33:07Z | - |
dc.date.available | 2016-09-20T05:33:07Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | ACS Infectious Diseases, 2016, v. 2 n. 7, p. 471-477 | - |
dc.identifier.issn | 2373-8227 | - |
dc.identifier.uri | http://hdl.handle.net/10722/232879 | - |
dc.description.abstract | Influenza viruses are obligate parasites that hijack the host cellular system. Previous results have shown that the influenza virus PB2 subunit confers a dependence of host eukaryotic translation initiation factor 4-γ 1 (eIF4G1) for viral mRNA translation. Here, we demonstrated that peptide-mediated interference of the PB2-eIF4G1 interaction inhibited virus replication in vitro and in vivo. Remarkably, intranasal administration of the peptide provided 100% protection against lethal challenges of influenza A viruses in BALB/c mice, including H1N1, H5N1, and H7N9 influenza virus subtypes. Mapping of the PB2 protein indicated that the eIF4G1 binding sites resided within the PB2 cap-binding domain. Virtual docking analysis suggested that the inhibitory peptide associated with the conserved amino acid residues that were essential to PB2 cap-binding activity. Overall, our results identified the PB2-eIF4G1 interactive site as a druggable target for influenza therapeutics. | - |
dc.language | eng | - |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/aidcbc | - |
dc.relation.ispartof | ACS Infectious Diseases | - |
dc.subject | Influenza virus | - |
dc.subject | Antiviral peptide | - |
dc.subject | Host−virus interaction | - |
dc.subject | eIF4G1 | - |
dc.subject | PB2 | - |
dc.subject | Tat | - |
dc.title | Peptide-Mediated Interference of PB2-eIF4G1 Interaction Inhibits Influenza A Viruses’ Replication in Vitro and in Vivo | - |
dc.type | Article | - |
dc.identifier.email | Yuan, S: yuansf@hku.hk | - |
dc.identifier.email | Chu, H: hinchu@hku.hk | - |
dc.identifier.email | Ye, J: yejiahui@hku.hk | - |
dc.identifier.email | Hu, M: meng16hu@hku.hk | - |
dc.identifier.email | Chow, BKC: bkcc@hku.hk | - |
dc.identifier.email | Zhou, J: jiezhou@hku.hk | - |
dc.identifier.email | Zheng, B: bzheng@hkucc.hku.hk | - |
dc.identifier.authority | Yuan, S=rp02640 | - |
dc.identifier.authority | Chu, H=rp02125 | - |
dc.identifier.authority | Chow, BKC=rp00681 | - |
dc.identifier.authority | Zhou, J=rp01412 | - |
dc.identifier.authority | Zheng, B=rp00353 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1021/acsinfecdis.6b00064 | - |
dc.identifier.pmid | 27626099 | - |
dc.identifier.scopus | eid_2-s2.0-84991523589 | - |
dc.identifier.hkuros | 263804 | - |
dc.identifier.volume | 2 | - |
dc.identifier.issue | 7 | - |
dc.identifier.spage | 471 | - |
dc.identifier.epage | 477 | - |
dc.identifier.isi | WOS:000379638600005 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 2373-8227 | - |