Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.
Identifieur interne : 000F15 ( PubMed/Corpus ); précédent : 000F14; suivant : 000F16Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.
Auteurs : Shan Su ; Yun Zhu ; Sheng Ye ; Qianqian Qi ; Shuai Xia ; Zhenxuan Ma ; Fei Yu ; Qian Wang ; Rongguang Zhang ; Shibo Jiang ; Lu LuSource :
- Journal of virology [ 1098-5514 ] ; 2017.
English descriptors
- KwdEn :
- Amino Acid Sequence, Cell Line, Tumor, Crystallography, X-Ray, Drug Design, Enfuvirtide, HIV Envelope Protein gp41 (chemical synthesis), HIV Envelope Protein gp41 (pharmacology), HIV Fusion Inhibitors (chemical synthesis), HIV Fusion Inhibitors (pharmacology), HIV-1 (chemistry), HIV-1 (drug effects), HIV-1 (growth & development), HIV-1 (metabolism), Humans, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Neuroglia (drug effects), Neuroglia (immunology), Neuroglia (virology), Peptide Fragments (chemical synthesis), Peptide Fragments (pharmacology), Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Secondary, Sequence Alignment, Structure-Activity Relationship, T-Lymphocytes (drug effects), T-Lymphocytes (immunology), T-Lymphocytes (virology), Virus Internalization (drug effects).
- MESH :
- chemical , chemical synthesis : HIV Envelope Protein gp41, HIV Fusion Inhibitors, Peptide Fragments.
- chemical , pharmacology : HIV Envelope Protein gp41, HIV Fusion Inhibitors, Peptide Fragments.
- chemical : Enfuvirtide.
- chemistry : HIV-1.
- drug effects : HIV-1, Neuroglia, T-Lymphocytes, Virus Internalization.
- growth & development : HIV-1.
- immunology : Neuroglia, T-Lymphocytes.
- metabolism : HIV-1.
- virology : Neuroglia, T-Lymphocytes.
- Amino Acid Sequence, Cell Line, Tumor, Crystallography, X-Ray, Drug Design, Humans, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Secondary, Sequence Alignment, Structure-Activity Relationship.
Abstract
20 (enfuvirtide) and other peptides derived from the human immunodeficiency virus type 1 (HIV-1) gp41 C-terminal heptad repeat (CHR) region inhibit HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. Several strategies focusing on the binding grooves of the NHR trimer have been adopted to increase the antiviral activity of the CHR peptides. Here, we developed a novel and simple strategy to greatly enhance the potency of the existing peptide-based HIV fusion inhibitors. First, we identified a shallow pocket adjacent to the groove in the N-terminal region of NHR trimer as a new drug target, and then we designed several short artificial peptides to fit this target. After the addition of IDL (Ile-Asp-Leu) to the C terminus of CHR peptide WQ or MT-WQ, the conjugated peptides, WQ-IDL and MT-WQ-IDL, showed much more potent activities than WQ and T20, respectively, in inhibiting HIV-1 IIIB infection. WQ-IDL and MT-WQ-IDL were also more effective than WQ in blocking HIV-1 Env-mediated membrane fusion and had higher levels of binding affinity with NHR peptide N46. We solved the crystal structure of the 6-HB formed by MT-WQ-IDL and N46 and found that, besides the N-terminal MT hook tail, the IDL tail anchor of MT-WQ-IDL also binds with the shallow hydrophobic pocket outside the groove of the NHR trimer, resulting in enhanced inhibition of HIV-1 fusion with the target cell. It is expected that this novel approach can be widely used to improve the potency of peptidic fusion inhibitors against other enveloped viruses with class I fusion proteins.
DOI: 10.1128/JVI.01445-16
PubMed: 27795416
Links to Exploration step
pubmed:27795416Le document en format XML
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<front><div type="abstract" xml:lang="en">20 (enfuvirtide) and other peptides derived from the human immunodeficiency virus type 1 (HIV-1) gp41 C-terminal heptad repeat (CHR) region inhibit HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. Several strategies focusing on the binding grooves of the NHR trimer have been adopted to increase the antiviral activity of the CHR peptides. Here, we developed a novel and simple strategy to greatly enhance the potency of the existing peptide-based HIV fusion inhibitors. First, we identified a shallow pocket adjacent to the groove in the N-terminal region of NHR trimer as a new drug target, and then we designed several short artificial peptides to fit this target. After the addition of IDL (Ile-Asp-Leu) to the C terminus of CHR peptide WQ or MT-WQ, the conjugated peptides, WQ-IDL and MT-WQ-IDL, showed much more potent activities than WQ and T20, respectively, in inhibiting HIV-1 IIIB infection. WQ-IDL and MT-WQ-IDL were also more effective than WQ in blocking HIV-1 Env-mediated membrane fusion and had higher levels of binding affinity with NHR peptide N46. We solved the crystal structure of the 6-HB formed by MT-WQ-IDL and N46 and found that, besides the N-terminal MT hook tail, the IDL tail anchor of MT-WQ-IDL also binds with the shallow hydrophobic pocket outside the groove of the NHR trimer, resulting in enhanced inhibition of HIV-1 fusion with the target cell. It is expected that this novel approach can be widely used to improve the potency of peptidic fusion inhibitors against other enveloped viruses with class I fusion proteins.</div>
</front>
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<DateCompleted><Year>2017</Year>
<Month>05</Month>
<Day>15</Day>
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<Month>03</Month>
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<ArticleTitle>Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.</ArticleTitle>
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<Abstract><AbstractText>20 (enfuvirtide) and other peptides derived from the human immunodeficiency virus type 1 (HIV-1) gp41 C-terminal heptad repeat (CHR) region inhibit HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation. Several strategies focusing on the binding grooves of the NHR trimer have been adopted to increase the antiviral activity of the CHR peptides. Here, we developed a novel and simple strategy to greatly enhance the potency of the existing peptide-based HIV fusion inhibitors. First, we identified a shallow pocket adjacent to the groove in the N-terminal region of NHR trimer as a new drug target, and then we designed several short artificial peptides to fit this target. After the addition of IDL (Ile-Asp-Leu) to the C terminus of CHR peptide WQ or MT-WQ, the conjugated peptides, WQ-IDL and MT-WQ-IDL, showed much more potent activities than WQ and T20, respectively, in inhibiting HIV-1 IIIB infection. WQ-IDL and MT-WQ-IDL were also more effective than WQ in blocking HIV-1 Env-mediated membrane fusion and had higher levels of binding affinity with NHR peptide N46. We solved the crystal structure of the 6-HB formed by MT-WQ-IDL and N46 and found that, besides the N-terminal MT hook tail, the IDL tail anchor of MT-WQ-IDL also binds with the shallow hydrophobic pocket outside the groove of the NHR trimer, resulting in enhanced inhibition of HIV-1 fusion with the target cell. It is expected that this novel approach can be widely used to improve the potency of peptidic fusion inhibitors against other enveloped viruses with class I fusion proteins.</AbstractText>
<AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">The hydrophobic groove of the human immunodeficiency virus type 1 (HIV-1) gp41 NHR trimer has been known as the classic drug target to develop fusion inhibitors derived from the gp41 CHR. Here, we developed a novel and simple strategy to improve the existing peptide-based HIV fusion inhibitors. We identified a shallow pocket adjacent to the groove in the NHR trimer and added a short artificial peptide consisting of three amino acids (IDL) to the C terminus of a fusion inhibitor to fit this new target. The inhibition activity of this new conjugated peptide was significantly enhanced, by 77-fold, making it much more potent than T20 (enfuvirtide) and suggesting that the IDL tail can be adopted for optimizing existing HIV-1 CHR peptide fusion inhibitors. This new approach of identifying a potential binding pocket outside the traditional target and creating an artificial tail anchor can be widely applied to design novel fusion inhibitors against other class I enveloped viruses, such as Middle East respiratory syndrome coronavirus (MERS-CoV).</AbstractText>
<CopyrightInformation>Copyright © 2016 American Society for Microbiology.</CopyrightInformation>
</Abstract>
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<ForeName>Shan</ForeName>
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<AffiliationInfo><Affiliation>National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation>
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<AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York, USA.</Affiliation>
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<ForeName>Lu</ForeName>
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<ArticleIdList><ArticleId IdType="pubmed">27795416</ArticleId>
<ArticleId IdType="pii">JVI.01445-16</ArticleId>
<ArticleId IdType="doi">10.1128/JVI.01445-16</ArticleId>
<ArticleId IdType="pmc">PMC5165219</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>FASEB J. 2013 Mar;27(3):1203-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23233535</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antimicrob Agents Chemother. 2009 Mar;53(3):1013-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19114674</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2014 Mar 4;111(9):3425-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24550514</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2012 Feb 24;287(9):6788-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22228771</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1997 Apr 18;89(2):263-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9108481</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19461840</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Angew Chem Int Ed Engl. 2002 Aug 16;41(16):2937-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12203417</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Neuroinflammation. 2013 Jul 31;10:98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23902750</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Oct 31;283(44):30376-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18662985</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2009 Jun 05;4(6):e5819</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19503790</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Retrovirology. 2012 Dec 07;9:104</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23217195</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2008 Oct 21;105(42):16332-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18852475</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2015 Jul;89(13):6960-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25903343</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Sci Rep. 2015 Aug 19;5:13028</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26286358</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2005 Sep 28;127(38):13126-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16173723</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1993 Sep 9;365(6442):113</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8371754</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Mar 25;280(12):11259-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15640162</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2003 May;77(9):5054-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12692208</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Pathog. 2010 May 06;6(5):e1000880</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20463810</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virol J. 2006 May 25;3:36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16725045</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Antimicrob Chemother. 2013 Nov;68(11):2533-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23794600</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Pharm Des. 2015;21(7):925-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25312722</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12772-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17640899</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2011 Oct;85(20):10785-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21835789</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2003 May 29;348(22):2175-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12637625</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Emerg Microbes Infect. 2016 Jun 22;5:e65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27329850</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>ChemMedChem. 2010 Nov 8;5(11):1813-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20845360</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol Struct Dyn. 1997 Dec;15(3):465-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9439994</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20124702</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Org Lett. 2002 Nov 14;4(23):4167-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12423113</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15613-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9861018</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2012 Dec;1818(12):2950-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22867851</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1988 Aug;85(16):6132-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2457906</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2011 Mar 15;411(2):251-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21247613</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2000 Apr 2;270(1):153-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10733920</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2013 Dec;87(24):13134-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24067982</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 2015 Apr;61(3-4):235-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25631354</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1997 May 22;387(6631):426-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9163431</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Fitoterapia. 2012 Mar;83(2):348-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22155187</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Nov;82(22):11129-39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18768964</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2004 Jun 29;43(25):8230-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15209519</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 1998 Nov;4(11):1302-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9809555</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Antimicrob Chemother. 2014 Oct;69(10):2759-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24908047</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Antimicrob Chemother. 2013 Mar;68(3):573-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23221626</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antimicrob Agents Chemother. 2009 Dec;53(12):4987-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19786602</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Mar 30;282(13):9612-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17276993</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Rep. 2015 Sep 8;12(10):1555-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26321639</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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