New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides.
Influenza A viral (IAV) fusion peptides are known for their important role in viral-cell fusion process and membrane destabilization potential which are compatible with those of antimicrobial peptides. Thus, by replacing the negatively or neutrally charged residues of FPs with positively charged lys...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4575187?pdf=render |
| _version_ | 1818032237142081536 |
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| author | Wenjiao Wu Dongguo Lin Xintian Shen Fangfang Li Yuxin Fang Kaiqun Li Tianrong Xun Guang Yang Jie Yang Shuwen Liu Jian He |
| author_facet | Wenjiao Wu Dongguo Lin Xintian Shen Fangfang Li Yuxin Fang Kaiqun Li Tianrong Xun Guang Yang Jie Yang Shuwen Liu Jian He |
| author_sort | Wenjiao Wu |
| collection | DOAJ |
| description | Influenza A viral (IAV) fusion peptides are known for their important role in viral-cell fusion process and membrane destabilization potential which are compatible with those of antimicrobial peptides. Thus, by replacing the negatively or neutrally charged residues of FPs with positively charged lysines, we synthesized several potent antimicrobial peptides derived from the fusogenic peptides (FPs) of hemagglutinin glycoproteins (HAs) of IAV. The biological screening identified that in addition to the potent antibacterial activities, these positively charged fusion peptides (pFPs) effectively inhibited the replication of influenza A viruses including oseltamivir-resistant strain. By employing pseudovirus-based entry inhibition assays including H5N1 influenza A virus (IAV), and VSV-G, the mechanism study indicated that the antiviral activity may be associated with the interactions between the HA2 subunit and pFP, of which, the nascent pFP exerted a strong effect to interrupt the conformational changes of HA2, thereby blocking the entry of viruses into host cells. In addition to providing new peptide "entry blockers", these data also demonstrate a useful strategy in designing potent antibacterial agents, as well as effective viral entry inhibitors. It would be meaningful in treatment of bacterial co-infection during influenza pandemic periods, as well as in our current war against those emerging pathogenic microorganisms such as IAV and HIV. |
| first_indexed | 2024-12-10T06:04:10Z |
| format | Article |
| id | doaj.art-6deff2c9a2244a27980af57791e5ee38 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-10T06:04:10Z |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-6deff2c9a2244a27980af57791e5ee382022-12-22T01:59:44ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01109e013842610.1371/journal.pone.0138426New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides.Wenjiao WuDongguo LinXintian ShenFangfang LiYuxin FangKaiqun LiTianrong XunGuang YangJie YangShuwen LiuJian HeInfluenza A viral (IAV) fusion peptides are known for their important role in viral-cell fusion process and membrane destabilization potential which are compatible with those of antimicrobial peptides. Thus, by replacing the negatively or neutrally charged residues of FPs with positively charged lysines, we synthesized several potent antimicrobial peptides derived from the fusogenic peptides (FPs) of hemagglutinin glycoproteins (HAs) of IAV. The biological screening identified that in addition to the potent antibacterial activities, these positively charged fusion peptides (pFPs) effectively inhibited the replication of influenza A viruses including oseltamivir-resistant strain. By employing pseudovirus-based entry inhibition assays including H5N1 influenza A virus (IAV), and VSV-G, the mechanism study indicated that the antiviral activity may be associated with the interactions between the HA2 subunit and pFP, of which, the nascent pFP exerted a strong effect to interrupt the conformational changes of HA2, thereby blocking the entry of viruses into host cells. In addition to providing new peptide "entry blockers", these data also demonstrate a useful strategy in designing potent antibacterial agents, as well as effective viral entry inhibitors. It would be meaningful in treatment of bacterial co-infection during influenza pandemic periods, as well as in our current war against those emerging pathogenic microorganisms such as IAV and HIV.http://europepmc.org/articles/PMC4575187?pdf=render |
| spellingShingle | Wenjiao Wu Dongguo Lin Xintian Shen Fangfang Li Yuxin Fang Kaiqun Li Tianrong Xun Guang Yang Jie Yang Shuwen Liu Jian He New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides. PLoS ONE |
| title | New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides. |
| title_full | New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides. |
| title_fullStr | New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides. |
| title_full_unstemmed | New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides. |
| title_short | New influenza A Virus Entry Inhibitors Derived from the Viral Fusion Peptides. |
| title_sort | new influenza a virus entry inhibitors derived from the viral fusion peptides |
| url | http://europepmc.org/articles/PMC4575187?pdf=render |
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