Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor.
Identifieur interne : 001576 ( Ncbi/Checkpoint ); précédent : 001575; suivant : 001577Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor.
Auteurs : John S. Mills [États-Unis]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Cellules CHO, Cinétique, Conformation des protéines, Coronavirus humain 229E (), Cricetinae, Données de séquences moléculaires, Ebolavirus (), Fragments peptidiques (), Fragments peptidiques (métabolisme), Guanosine 5'-O-(3-thiotriphosphate) (métabolisme), Humains, Liaison aux protéines, Modèles moléculaires, Protéines virales (), Protéines virales (métabolisme), Récepteurs aux peptides formylés (métabolisme), Sites de fixation, Séquence d'acides aminés, Transfection, VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (), VIH-2 (Virus de l'Immunodéficience Humaine de type 2) (), Virus du SRAS ().
- MESH :
- métabolisme : Fragments peptidiques, Guanosine 5'-O-(3-thiotriphosphate), Protéines virales, Récepteurs aux peptides formylés.
- Animaux, Cellules CHO, Cinétique, Conformation des protéines, Coronavirus humain 229E, Cricetinae, Données de séquences moléculaires, Ebolavirus, Fragments peptidiques, Humains, Liaison aux protéines, Modèles moléculaires, Protéines virales, Sites de fixation, Séquence d'acides aminés, Transfection, VIH-1 (Virus de l'Immunodéficience Humaine de type 1), VIH-2 (Virus de l'Immunodéficience Humaine de type 2), Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, CHO Cells, Coronavirus 229E, Human (chemistry), Cricetinae, Ebolavirus (chemistry), Guanosine 5'-O-(3-Thiotriphosphate) (metabolism), HIV-1 (chemistry), HIV-2 (chemistry), Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Peptide Fragments (chemistry), Peptide Fragments (metabolism), Protein Binding, Protein Conformation, Receptors, Formyl Peptide (metabolism), SARS Virus (chemistry), Transfection, Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Peptide Fragments, Viral Proteins.
- chemical , metabolism : Guanosine 5'-O-(3-Thiotriphosphate), Peptide Fragments, Receptors, Formyl Peptide, Viral Proteins.
- chemistry : Coronavirus 229E, Human, Ebolavirus, HIV-1, HIV-2, SARS Virus.
- Amino Acid Sequence, Animals, Binding Sites, CHO Cells, Cricetinae, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Transfection.
Abstract
Peptides derived from the membrane proximal region of fusion proteins of human immunodeficiency viruses 1 and 2, Coronavirus 229 E, severe acute respiratory syndrome coronavirus and Ebola virus were all potent antagonists of the formyl peptide receptor expressed in Chinese hamster ovary cells. Binding of viral peptides was affected by the naturally occurring polymorphisms at residues 190 and 192, which are located at second extracellular loop-transmembrane helix 5 interface. Substitution of R190 with W190 enhanced the affinity for a severe acute respiratory syndrome coronavirus peptide 6 fold but reduced the affinity for N-formyl-Nle-Leu-Phe by 2.5 fold. A 12 mer peptide derived from coronavirus 229E (ETYIKPWWVWL) was the most potent antagonist of the formyl peptide receptor W190 with a K(i) of 230 nM. Fluorescently labeled ETYIKPWWVWL was effectively internalized by all three variants with EC(50) of approximately 25 nM. An HKU-1 coronavirus peptide, MYVKWPWYVWL, was a potent antagonist but N-formyl-MYVKWPWYVWL was a potent agonist. ETYIKPWWVWL did not stimulate GTPgammaS binding but inhibited the stimulation by formyl-NleLeuPhe. It also blocked beta arrestin translocation and receptor downregulation induced by formyl-Nle-Leu-Phe. This indicates that formyl peptide receptor may be important in viral infections and that variations in its sequence among individuals may affect their likelihood of viral and bacterial infections.
DOI: 10.1016/j.bbadis.2006.05.008
PubMed: 16842982
Affiliations:
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Mills</name><affiliation wicri:level="2"><nlm:affiliation>109 Lewis Hall, Montana State University, Bozeman, MT 59717-3520, USA. umbmj@montana.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>109 Lewis Hall, Montana State University, Bozeman, MT 59717-3520</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16842982</idno><idno type="pmid">16842982</idno><idno type="doi">10.1016/j.bbadis.2006.05.008</idno><idno type="wicri:Area/PubMed/Corpus">002166</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002166</idno><idno type="wicri:Area/PubMed/Curation">002166</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002166</idno><idno type="wicri:Area/PubMed/Checkpoint">002071</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002071</idno><idno type="wicri:Area/Ncbi/Merge">001576</idno><idno type="wicri:Area/Ncbi/Curation">001576</idno><idno type="wicri:Area/Ncbi/Checkpoint">001576</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor.</title><author><name sortKey="Mills, John S" sort="Mills, John S" uniqKey="Mills J" first="John S" last="Mills">John S. Mills</name><affiliation wicri:level="2"><nlm:affiliation>109 Lewis Hall, Montana State University, Bozeman, MT 59717-3520, USA. umbmj@montana.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>109 Lewis Hall, Montana State University, Bozeman, MT 59717-3520</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></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>Animals</term><term>Binding Sites</term><term>CHO Cells</term><term>Coronavirus 229E, Human (chemistry)</term><term>Cricetinae</term><term>Ebolavirus (chemistry)</term><term>Guanosine 5'-O-(3-Thiotriphosphate) (metabolism)</term><term>HIV-1 (chemistry)</term><term>HIV-2 (chemistry)</term><term>Humans</term><term>Kinetics</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Receptors, Formyl Peptide (metabolism)</term><term>SARS Virus (chemistry)</term><term>Transfection</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules CHO</term><term>Cinétique</term><term>Conformation des protéines</term><term>Coronavirus humain 229E ()</term><term>Cricetinae</term><term>Données de séquences moléculaires</term><term>Ebolavirus ()</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (métabolisme)</term><term>Guanosine 5'-O-(3-thiotriphosphate) (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Protéines virales ()</term><term>Protéines virales (métabolisme)</term><term>Récepteurs aux peptides formylés (métabolisme)</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Transfection</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) ()</term><term>VIH-2 (Virus de l'Immunodéficience Humaine de type 2) ()</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Fragments</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Guanosine 5'-O-(3-Thiotriphosphate)</term><term>Peptide Fragments</term><term>Receptors, Formyl Peptide</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus 229E, Human</term><term>Ebolavirus</term><term>HIV-1</term><term>HIV-2</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fragments peptidiques</term><term>Guanosine 5'-O-(3-thiotriphosphate)</term><term>Protéines virales</term><term>Récepteurs aux peptides formylés</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>CHO Cells</term><term>Cricetinae</term><term>Humans</term><term>Kinetics</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Conformation</term><term>Transfection</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules CHO</term><term>Cinétique</term><term>Conformation des protéines</term><term>Coronavirus humain 229E</term><term>Cricetinae</term><term>Données de séquences moléculaires</term><term>Ebolavirus</term><term>Fragments peptidiques</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Protéines virales</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Transfection</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term><term>VIH-2 (Virus de l'Immunodéficience Humaine de type 2)</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Peptides derived from the membrane proximal region of fusion proteins of human immunodeficiency viruses 1 and 2, Coronavirus 229 E, severe acute respiratory syndrome coronavirus and Ebola virus were all potent antagonists of the formyl peptide receptor expressed in Chinese hamster ovary cells. Binding of viral peptides was affected by the naturally occurring polymorphisms at residues 190 and 192, which are located at second extracellular loop-transmembrane helix 5 interface. Substitution of R190 with W190 enhanced the affinity for a severe acute respiratory syndrome coronavirus peptide 6 fold but reduced the affinity for N-formyl-Nle-Leu-Phe by 2.5 fold. A 12 mer peptide derived from coronavirus 229E (ETYIKPWWVWL) was the most potent antagonist of the formyl peptide receptor W190 with a K(i) of 230 nM. Fluorescently labeled ETYIKPWWVWL was effectively internalized by all three variants with EC(50) of approximately 25 nM. An HKU-1 coronavirus peptide, MYVKWPWYVWL, was a potent antagonist but N-formyl-MYVKWPWYVWL was a potent agonist. ETYIKPWWVWL did not stimulate GTPgammaS binding but inhibited the stimulation by formyl-NleLeuPhe. It also blocked beta arrestin translocation and receptor downregulation induced by formyl-Nle-Leu-Phe. This indicates that formyl peptide receptor may be important in viral infections and that variations in its sequence among individuals may affect their likelihood of viral and bacterial infections.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Montana</li></region></list><tree><country name="États-Unis"><region name="Montana"><name sortKey="Mills, John S" sort="Mills, John S" uniqKey="Mills J" first="John S" last="Mills">John S. Mills</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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