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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pubmed:16290276Le document en format XML
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<term>HIV Fusion Inhibitors (pharmacology)</term>
<term>Hydrophobic and Hydrophilic Interactions</term>
<term>Liposomes</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Phosphatidylcholines</term>
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<term>Viral Fusion Proteins (chemistry)</term>
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<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>
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<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>
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<ReferenceList><Reference><Citation>Lancet. 2003 Apr 19;361(9366):1319-25</Citation>
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<tree><noCountry><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>
<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>
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<country name="Portugal"><noRegion><name sortKey="Veiga, Salome" sort="Veiga, Salome" uniqKey="Veiga S" first="Salomé" last="Veiga">Salomé Veiga</name>
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