Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions
Identifieur interne : 004557 ( Main/Exploration ); précédent : 004556; suivant : 004558Why are HIV-1 fusion inhibitors not effective against SARS-CoV? Biophysical evaluation of molecular interactions
Auteurs : Salomé Veiga [Portugal] ; Yunyun Yuan [République populaire de Chine] ; Xuqin Li [République populaire de Chine] ; Nuno C. Santos [Portugal] ; Gang Liu [République populaire de Chine] ; Miguel A. R. B. Castanho [Portugal]Source :
- Biochimica et Biophysica Acta. General Subjects [ 0304-4165 ] ; 2005.
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 (
Url:
DOI: 10.1016/j.bbagen.2005.10.001
PubMed: 16290276
PubMed Central: 7116955
Affiliations:
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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:aff id="aff1">Centro de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande C8, 1749-016 Lisboa, Portugal</nlm:aff><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><affiliation wicri:level="1"><nlm:aff id="aff2">Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, 1 Xian Nong Tan St., Beijing 100050, P. R. China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, 1 Xian Nong Tan St., Beijing 100050</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Li, Xuqin" sort="Li, Xuqin" uniqKey="Li X" first="Xuqin" last="Li">Xuqin Li</name><affiliation wicri:level="1"><nlm:aff id="aff2">Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, 1 Xian Nong Tan St., Beijing 100050, P. R. China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, 1 Xian Nong Tan St., Beijing 100050</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Santos, Nuno C" sort="Santos, Nuno C" uniqKey="Santos N" first="Nuno C." last="Santos">Nuno C. Santos</name><affiliation wicri:level="1"><nlm:aff id="aff3">Instituto de Biopatologia Química/Faculdade de Medicina de Lisboa and Unidade de Biopatologia Vascular/Instituto de Medicina Molecular, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal</nlm:aff><country xml:lang="fr">Portugal</country><wicri:regionArea>Instituto de Biopatologia Química/Faculdade de Medicina de Lisboa and Unidade de Biopatologia Vascular/Instituto de Medicina Molecular, Av. Prof. Egas Moniz, 1649-028 Lisboa</wicri:regionArea><wicri:noRegion>1649-028 Lisboa</wicri:noRegion></affiliation></author><author><name sortKey="Liu, Gang" sort="Liu, Gang" uniqKey="Liu G" first="Gang" last="Liu">Gang Liu</name><affiliation wicri:level="1"><nlm:aff id="aff2">Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, 1 Xian Nong Tan St., Beijing 100050, P. R. China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Chinese Academy of Medical Sciences and Peking Union Medical College, Institute of Materia Medica, 1 Xian Nong Tan St., Beijing 100050</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></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><affiliation wicri:level="1"><nlm:aff id="aff1">Centro de Química e Bioquímica, Faculdade de Ciências da Universidade de Lisboa, Campo Grande C8, 1749-016 Lisboa, Portugal</nlm:aff><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></analytic><series><title level="j">Biochimica et Biophysica Acta. General Subjects</title><idno type="ISSN">0304-4165</idno><idno type="eISSN">1872-8006</idno><imprint><date when="2005">2005</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"><p>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 (<italic>K</italic><sub>B</sub> = (1.1 ± 0.3) × 10<sup>5</sup> M<sup>−1</sup>). 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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Drosten, C" uniqKey="Drosten C">C. Drosten</name></author><author><name sortKey="Gunther, S" uniqKey="Gunther S">S. Günther</name></author><author><name sortKey="Preiser, W" uniqKey="Preiser W">W. Preiser</name></author><author><name sortKey="Van Der Werf, S" uniqKey="Van Der Werf S">S. van der Werf</name></author><author><name sortKey="Brodt, H" uniqKey="Brodt H">H. Brodt</name></author><author><name sortKey="Becker, S" uniqKey="Becker S">S. Becker</name></author><author><name sortKey="Rabenau, H" uniqKey="Rabenau H">H. Rabenau</name></author><author><name sortKey="Panning, M" uniqKey="Panning M">M. 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Santos</name></country><country name="République populaire de Chine"><noRegion><name sortKey="Yuan, Yunyun" sort="Yuan, Yunyun" uniqKey="Yuan Y" first="Yunyun" last="Yuan">Yunyun Yuan</name></noRegion><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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