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Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.

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Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.

Source :

Journal of virology [ 1098-5514 ] ; 2017.

RBID : pubmed:27795416

Descripteurs français

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

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<term>Cell Line, Tumor</term>
<term>Crystallography, X-Ray</term>
<term>Drug Design</term>
<term>Enfuvirtide</term>
<term>HIV Envelope Protein gp41 (chemical synthesis)</term>
<term>HIV Envelope Protein gp41 (pharmacology)</term>
<term>HIV Fusion Inhibitors (chemical synthesis)</term>
<term>HIV Fusion Inhibitors (pharmacology)</term>
<term>HIV-1 (chemistry)</term>
<term>HIV-1 (drug effects)</term>
<term>HIV-1 (growth & development)</term>
<term>HIV-1 (metabolism)</term>
<term>Humans</term>
<term>Hydrophobic and Hydrophilic Interactions</term>
<term>Models, Molecular</term>
<term>Neuroglia (drug effects)</term>
<term>Neuroglia (immunology)</term>
<term>Neuroglia (virology)</term>
<term>Peptide Fragments (chemical synthesis)</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Secondary</term>
<term>Sequence Alignment</term>
<term>Structure-Activity Relationship</term>
<term>T-Lymphocytes (drug effects)</term>
<term>T-Lymphocytes (immunology)</term>
<term>T-Lymphocytes (virology)</term>
<term>Virus Internalization (drug effects)</term>
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<term>Conception de médicament</term>
<term>Cristallographie aux rayons X</term>
<term>Fragments peptidiques (pharmacologie)</term>
<term>Fragments peptidiques (synthèse chimique)</term>
<term>Humains</term>
<term>Inhibiteurs de fusion du VIH (pharmacologie)</term>
<term>Inhibiteurs de fusion du VIH (synthèse chimique)</term>
<term>Interactions hydrophobes et hydrophiles</term>
<term>Lignée cellulaire tumorale</term>
<term>Lymphocytes T ()</term>
<term>Lymphocytes T (immunologie)</term>
<term>Lymphocytes T (virologie)</term>
<term>Modèles moléculaires</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Multimérisation de protéines</term>
<term>Névroglie ()</term>
<term>Névroglie (immunologie)</term>
<term>Névroglie (virologie)</term>
<term>Protéine d'enveloppe gp41 du VIH (pharmacologie)</term>
<term>Protéine d'enveloppe gp41 du VIH (synthèse chimique)</term>
<term>Pénétration virale ()</term>
<term>Relation structure-activité</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) ()</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (croissance et développement)</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>HIV Envelope Protein gp41</term>
<term>HIV Fusion Inhibitors</term>
<term>Peptide Fragments</term>
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<term>HIV Fusion Inhibitors</term>
<term>Peptide Fragments</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Enfuvirtide</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>HIV-1</term>
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<term>T-Lymphocytes</term>
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<term>Névroglie</term>
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<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Neuroglia</term>
<term>T-Lymphocytes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>HIV-1</term>
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<term>Inhibiteurs de fusion du VIH</term>
<term>Protéine d'enveloppe gp41 du VIH</term>
</keywords>
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<term>Sequence Alignment</term>
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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>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27795416</PMID>
<DateCompleted><Year>2017</Year>
<Month>05</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>03</Month>
<Day>29</Day>
</DateRevised>
<Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>91</Volume>
<Issue>1</Issue>
<PubDate><Year>2017</Year>
<Month>Jan</Month>
<Day>01</Day>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">e01445-16</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01445-16</ELocationID>
<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>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Su</LastName>
<ForeName>Shan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhu</LastName>
<ForeName>Yun</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ye</LastName>
<ForeName>Sheng</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qi</LastName>
<ForeName>Qianqian</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xia</LastName>
<ForeName>Shuai</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ma</LastName>
<ForeName>Zhenxuan</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yu</LastName>
<ForeName>Fei</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Qian</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Rongguang</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</Affiliation>
</AffiliationInfo>
<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>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jiang</LastName>
<ForeName>Shibo</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China shibojiang@fudan.edu.cn lul@fudan.edu.cn.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Lu</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences and Shanghai Public Health Clinical Center, Fudan University, Shanghai, China shibojiang@fudan.edu.cn lul@fudan.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>U01 AA020930</GrantID>
<Acronym>AA</Acronym>
<Agency>NIAAA NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>12</Month>
<Day>16</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D015700">HIV Envelope Protein gp41</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D023581">HIV Fusion Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>19OWO1T3ZE</RegistryNumber>
<NameOfSubstance UI="D000077560">Enfuvirtide</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015195" MajorTopicYN="Y">Drug Design</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000077560" MajorTopicYN="N">Enfuvirtide</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015700" MajorTopicYN="N">HIV Envelope Protein gp41</DescriptorName>
<QualifierName UI="Q000138" MajorTopicYN="Y">chemical synthesis</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
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<QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
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<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
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<QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName>
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<MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName>
<QualifierName UI="Q000138" MajorTopicYN="Y">chemical synthesis</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
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<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013601" MajorTopicYN="N">T-Lymphocytes</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
</MeshHeading>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">HIV</Keyword>
<Keyword MajorTopicYN="Y">fusion inhibitor</Keyword>
<Keyword MajorTopicYN="Y">gp41</Keyword>
<Keyword MajorTopicYN="Y">peptide</Keyword>
<Keyword MajorTopicYN="Y">six-helix bundle</Keyword>
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	Serveur d'exploration MERS
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Serveur d'exploration MERS

Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.

Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.

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