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Article: Peptide-Mediated Interference of PB2-eIF4G1 Interaction Inhibits Influenza A Viruses’ Replication in Vitro and in Vivo

TitlePeptide-Mediated Interference of PB2-eIF4G1 Interaction Inhibits Influenza A Viruses’ Replication in Vitro and in Vivo
Authors
KeywordsInfluenza virus
Antiviral peptide
Host−virus interaction
eIF4G1
PB2
Tat
Issue Date2016
PublisherAmerican 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?
AbstractInfluenza 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 Identifierhttp://hdl.handle.net/10722/232879
ISSN
2017 Impact Factor: 4.325
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYuan, S-
dc.contributor.authorChu, H-
dc.contributor.authorYe, J-
dc.contributor.authorHu, M-
dc.contributor.authorSingh, K-
dc.contributor.authorChow, BKC-
dc.contributor.authorZhou, J-
dc.contributor.authorZheng, B-
dc.date.accessioned2016-09-20T05:33:07Z-
dc.date.available2016-09-20T05:33:07Z-
dc.date.issued2016-
dc.identifier.citationACS Infectious Diseases, 2016, v. 2 n. 7, p. 471-477-
dc.identifier.issn2373-8227-
dc.identifier.urihttp://hdl.handle.net/10722/232879-
dc.description.abstractInfluenza 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.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/aidcbc-
dc.relation.ispartofACS Infectious Diseases-
dc.subjectInfluenza virus-
dc.subjectAntiviral peptide-
dc.subjectHost−virus interaction-
dc.subjecteIF4G1-
dc.subjectPB2-
dc.subjectTat-
dc.titlePeptide-Mediated Interference of PB2-eIF4G1 Interaction Inhibits Influenza A Viruses’ Replication in Vitro and in Vivo-
dc.typeArticle-
dc.identifier.emailYuan, S: yuansf@hku.hk-
dc.identifier.emailChu, H: hinchu@hku.hk-
dc.identifier.emailYe, J: yejiahui@hku.hk-
dc.identifier.emailHu, M: meng16hu@hku.hk-
dc.identifier.emailChow, BKC: bkcc@hku.hk-
dc.identifier.emailZhou, J: jiezhou@hku.hk-
dc.identifier.emailZheng, B: bzheng@hkucc.hku.hk-
dc.identifier.authorityYuan, S=rp02640-
dc.identifier.authorityChu, H=rp02125-
dc.identifier.authorityChow, BKC=rp00681-
dc.identifier.authorityZhou, J=rp01412-
dc.identifier.authorityZheng, B=rp00353-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/acsinfecdis.6b00064-
dc.identifier.pmid27626099-
dc.identifier.scopuseid_2-s2.0-84991523589-
dc.identifier.hkuros263804-
dc.identifier.volume2-
dc.identifier.issue7-
dc.identifier.spage471-
dc.identifier.epage477-
dc.identifier.isiWOS:000379638600005-
dc.publisher.placeUnited States-

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