Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions.
Identifieur interne : 001F23 ( PubMed/Checkpoint ); précédent : 001F22; suivant : 001F24Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions.
Auteurs : Salomé Veiga [Portugal] ; Yunyun Yuan ; Xuqin Li ; Nuno C. Santos ; Gang Liu ; Miguel A R B. CastanhoSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Fusion Proteins.
- chemical , pharmacology : HIV Envelope Protein gp41, HIV Fusion Inhibitors, Peptide Fragments.
- chemical : Enfuvirtide, Liposomes, Phosphatidylcholines.
- drug effects : SARS Virus.
- Amino Acid Sequence, Hydrophobic and Hydrophilic Interactions.
Abstract
The envelope spike (S) glycoprotein of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) mediates the entry of the virus into target cells. Recent studies point out to a cell entry mechanism of this virus similar to other enveloped viruses, such as HIV-1. As it happens with other viruses peptidic fusion inhibitors, SARS-CoV S protein HR2-derived peptides are potential therapeutic drugs against the virus. It is believed that HR2 peptides block the six-helix bundle formation, a key structure in the viral fusion, by interacting with the HR1 region. It is a matter of discussion if the HIV-1 gp41 HR2-derived peptide T20 (enfuvirtide) could be a possible SARS-CoV inhibitor given the similarities between the two viruses. We tested the possibility of interaction between both T20 (HIV-1 gp41 HR2-derived peptide) and T-1249 with S protein HR1- and HR2-derived peptides. Our biophysical data show a significant interaction between a SARS-CoV HR1-derived peptide and T20. However, the interaction is only moderate (K(B)=(1.1+/-0.3)x10(5) M(-1)). This finding shows that the reasoning behind the hypothesis that T20, already approved for clinical application in AIDS treatment, could inhibit the fusion of SARS-CoV with target cells is correct but the effect may not be strong enough for application.
DOI: 10.1016/j.bbagen.2005.10.001
PubMed: 16290276
Affiliations:
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Santos</name></author><author><name sortKey="Liu, Gang" sort="Liu, Gang" uniqKey="Liu G" first="Gang" last="Liu">Gang Liu</name></author><author><name sortKey="Castanho, Miguel A R B" sort="Castanho, Miguel A R B" uniqKey="Castanho M" first="Miguel A R B" last="Castanho">Miguel A R B. 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Biophysical evaluation of molecular interactions.</title><author><name sortKey="Veiga, Salome" sort="Veiga, Salome" uniqKey="Veiga S" first="Salomé" last="Veiga">Salomé Veiga</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande C8, 1749-016 Lisboa, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>Centro de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande C8, 1749-016 Lisboa</wicri:regionArea><wicri:noRegion>1749-016 Lisboa</wicri:noRegion></affiliation></author><author><name sortKey="Yuan, Yunyun" sort="Yuan, Yunyun" uniqKey="Yuan Y" first="Yunyun" last="Yuan">Yunyun Yuan</name></author><author><name sortKey="Li, Xuqin" sort="Li, Xuqin" uniqKey="Li X" first="Xuqin" last="Li">Xuqin Li</name></author><author><name sortKey="Santos, Nuno C" sort="Santos, Nuno C" uniqKey="Santos N" first="Nuno C" last="Santos">Nuno C. Santos</name></author><author><name sortKey="Liu, Gang" sort="Liu, Gang" uniqKey="Liu G" first="Gang" last="Liu">Gang Liu</name></author><author><name sortKey="Castanho, Miguel A R B" sort="Castanho, Miguel A R B" uniqKey="Castanho M" first="Miguel A R B" last="Castanho">Miguel A R B. Castanho</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Enfuvirtide</term><term>HIV Envelope Protein gp41 (pharmacology)</term><term>HIV Fusion Inhibitors (pharmacology)</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Liposomes</term><term>Peptide Fragments (pharmacology)</term><term>Phosphatidylcholines</term><term>SARS Virus (drug effects)</term><term>Viral Fusion Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fragments peptidiques (pharmacologie)</term><term>Inhibiteurs de fusion du VIH (pharmacologie)</term><term>Interactions hydrophobes et hydrophiles</term><term>Liposomes</term><term>Phosphatidylcholines</term><term>Protéine d'enveloppe gp41 du VIH (pharmacologie)</term><term>Protéines de fusion virale ()</term><term>Séquence d'acides aminés</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>HIV Envelope Protein gp41</term><term>HIV Fusion Inhibitors</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Enfuvirtide</term><term>Liposomes</term><term>Phosphatidylcholines</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Fragments peptidiques</term><term>Inhibiteurs de fusion du VIH</term><term>Protéine d'enveloppe gp41 du VIH</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Hydrophobic and Hydrophilic Interactions</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Interactions hydrophobes et hydrophiles</term><term>Liposomes</term><term>Phosphatidylcholines</term><term>Protéines de fusion virale</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The envelope spike (S) glycoprotein of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) mediates the entry of the virus into target cells. Recent studies point out to a cell entry mechanism of this virus similar to other enveloped viruses, such as HIV-1. As it happens with other viruses peptidic fusion inhibitors, SARS-CoV S protein HR2-derived peptides are potential therapeutic drugs against the virus. It is believed that HR2 peptides block the six-helix bundle formation, a key structure in the viral fusion, by interacting with the HR1 region. It is a matter of discussion if the HIV-1 gp41 HR2-derived peptide T20 (enfuvirtide) could be a possible SARS-CoV inhibitor given the similarities between the two viruses. We tested the possibility of interaction between both T20 (HIV-1 gp41 HR2-derived peptide) and T-1249 with S protein HR1- and HR2-derived peptides. Our biophysical data show a significant interaction between a SARS-CoV HR1-derived peptide and T20. However, the interaction is only moderate (K(B)=(1.1+/-0.3)x10(5) M(-1)). This finding shows that the reasoning behind the hypothesis that T20, already approved for clinical application in AIDS treatment, could inhibit the fusion of SARS-CoV with target cells is correct but the effect may not be strong enough for application.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16290276</PMID><DateCompleted><Year>2006</Year><Month>06</Month><Day>09</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1760</Volume><Issue>1</Issue><PubDate><Year>2006</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation></Journal><ArticleTitle>Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions.</ArticleTitle><Pagination><MedlinePgn>55-61</MedlinePgn></Pagination><Abstract><AbstractText>The envelope spike (S) glycoprotein of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) mediates the entry of the virus into target cells. Recent studies point out to a cell entry mechanism of this virus similar to other enveloped viruses, such as HIV-1. As it happens with other viruses peptidic fusion inhibitors, SARS-CoV S protein HR2-derived peptides are potential therapeutic drugs against the virus. It is believed that HR2 peptides block the six-helix bundle formation, a key structure in the viral fusion, by interacting with the HR1 region. It is a matter of discussion if the HIV-1 gp41 HR2-derived peptide T20 (enfuvirtide) could be a possible SARS-CoV inhibitor given the similarities between the two viruses. We tested the possibility of interaction between both T20 (HIV-1 gp41 HR2-derived peptide) and T-1249 with S protein HR1- and HR2-derived peptides. Our biophysical data show a significant interaction between a SARS-CoV HR1-derived peptide and T20. However, the interaction is only moderate (K(B)=(1.1+/-0.3)x10(5) M(-1)). This finding shows that the reasoning behind the hypothesis that T20, already approved for clinical application in AIDS treatment, could inhibit the fusion of SARS-CoV with target cells is correct but the effect may not be strong enough for application.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Veiga</LastName><ForeName>Salomé</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centro de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande C8, 1749-016 Lisboa, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yuan</LastName><ForeName>Yunyun</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xuqin</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Santos</LastName><ForeName>Nuno C</ForeName><Initials>NC</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Gang</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Castanho</LastName><ForeName>Miguel A R B</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>10</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</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="D008081">Liposomes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010713">Phosphatidylcholines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014760">Viral Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C474741">peptide T1249</NameOfSubstance></Chemical><Chemical><RegistryNumber>19OWO1T3ZE</RegistryNumber><NameOfSubstance UI="D000077560">Enfuvirtide</NameOfSubstance></Chemical><Chemical><RegistryNumber>TE895536Y5</RegistryNumber><NameOfSubstance 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Castanho</name><name sortKey="Li, Xuqin" sort="Li, Xuqin" uniqKey="Li X" first="Xuqin" last="Li">Xuqin Li</name><name sortKey="Liu, Gang" sort="Liu, Gang" uniqKey="Liu G" first="Gang" last="Liu">Gang Liu</name><name sortKey="Santos, Nuno C" sort="Santos, Nuno C" uniqKey="Santos N" first="Nuno C" last="Santos">Nuno C. Santos</name><name sortKey="Yuan, Yunyun" sort="Yuan, Yunyun" uniqKey="Yuan Y" first="Yunyun" last="Yuan">Yunyun Yuan</name></noCountry><country name="Portugal"><noRegion><name sortKey="Veiga, Salome" sort="Veiga, Salome" uniqKey="Veiga S" first="Salomé" last="Veiga">Salomé Veiga</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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