Reconstitution of the receptor-binding motif of the SARS coronavirus
Identifieur interne : 001263 ( Main/Exploration ); précédent : 001262; suivant : 001264Reconstitution of the receptor-binding motif of the SARS coronavirus
Auteurs : Natalia T. Freund [Israël, États-Unis] ; Anna Roitburd-Berman [Israël] ; Jianhua Sui [États-Unis, République populaire de Chine] ; Wayne A. Marasco [États-Unis] ; Jonathan M. Gershoni [Israël]Source :
- Protein Engineering, Design and Selection [ 1741-0126 ] ; 2015.
Descripteurs français
- KwdFr :
- Banque de peptides, Données de séquences moléculaires, Fragments peptidiques (), Fragments peptidiques (génétique), Fragments peptidiques (métabolisme), Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Modèles moléculaires, Motifs d'acides aminés (génétique), Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (métabolisme), Sites de fixation (génétique), Séquence d'acides aminés, Virus du SRAS (génétique).
- MESH :
- génétique : Fragments peptidiques, Glycoprotéine de spicule des coronavirus, Motifs d'acides aminés, Sites de fixation, Virus du SRAS.
- métabolisme : Fragments peptidiques, Glycoprotéine de spicule des coronavirus, Peptidyl-Dipeptidase A.
- Banque de peptides, Données de séquences moléculaires, Fragments peptidiques, Glycoprotéine de spicule des coronavirus, Humains, Modèles moléculaires, Peptidyl-Dipeptidase A, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs (genetics), Amino Acid Sequence, Binding Sites (genetics), Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments (chemistry), Peptide Fragments (genetics), Peptide Fragments (metabolism), Peptide Library, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (metabolism), SARS Virus (genetics), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism).
- MESH :
- chemical , chemistry : Peptide Fragments, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus.
- genetics : Amino Acid Motifs, Binding Sites, Peptide Fragments, SARS Virus, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Peptide Fragments, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus.
- Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, Peptide Library.
Abstract
The severe acute respiratory syndrome (SARS) coronavirus (CoV) identified in 2003 has infected ∼8000 people worldwide, killing nearly 10% of them. The infection of target cells by the SARS CoV is mediated through the interaction of the viral Spike (S) protein (1255 amino acids) and its cellular receptor, angiotensin-converting enzyme 2 (ACE2). The SARS CoV receptor-binding domain (amino acids N318–T509 of S protein) harbors an extended excursion along its periphery that contacts ACE2 and is designated the receptor-binding motif (RBM, amino acids S432–T486). In addition, the RBM is a major antigenic determinant, able to elicit production of neutralizing antibodies. Hence, the role of the RBM is a bi-functional bioactive surface that can be demonstrated by antibodies such as the neutralizing human anti-SARS monoclonal antibody (mAb) 80R which targets the RBM and competes with the ACE2 receptor for binding. Here, we employ phage-display peptide-libraries to reconstitute a functional RBM. This is achieved by generating a vast collection of candidate RBM peptides that present a diversity of conformations. Screening such ‘Conformer Libraries’ with corresponding ligands has produced short RBM constructs (ca. 40 amino acids) that can bind both the ACE2 receptor and the neutralizing mAb 80R.
Url:
DOI: 10.1093/protein/gzv052
PubMed: 26487711
PubMed Central: 7107155
Affiliations:
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Freund</name><affiliation wicri:level="1"><nlm:aff id="af1"><addr-line>Department of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences</addr-line>,<institution>Tel Aviv University</institution>,<addr-line>Tel Aviv 69978</addr-line>,<country>Israel</country></nlm:aff><country xml:lang="fr">Israël</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="af4"><addr-line>Present address: Laboratory of Molecular Immunology</addr-line>,<institution>The Rockefeller University</institution>,<addr-line>New York, NY 10065</addr-line>,<country>USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Roitburd Berman, Anna" sort="Roitburd Berman, Anna" uniqKey="Roitburd Berman A" first="Anna" last="Roitburd-Berman">Anna Roitburd-Berman</name><affiliation wicri:level="1"><nlm:aff id="af1"><addr-line>Department of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences</addr-line>,<institution>Tel Aviv University</institution>,<addr-line>Tel Aviv 69978</addr-line>,<country>Israel</country></nlm:aff><country xml:lang="fr">Israël</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Sui, Jianhua" sort="Sui, Jianhua" uniqKey="Sui J" first="Jianhua" last="Sui">Jianhua Sui</name><affiliation><nlm:aff id="af2"><addr-line>Department of Cancer Immunology and AIDS</addr-line>,<institution>Dana Farber Cancer Institute</institution></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af3"><addr-line>Department of Medicine</addr-line>,<institution>Harvard Medical School</institution>,<addr-line>Boston, MA 02115</addr-line>,<country>USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="af5"><institution>Present address: National Institute of Biological Sciences</institution>,<addr-line>Beijing 102206</addr-line>,<country>China</country></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Marasco, Wayne A" sort="Marasco, Wayne A" uniqKey="Marasco W" first="Wayne A." last="Marasco">Wayne A. Marasco</name><affiliation><nlm:aff id="af2"><addr-line>Department of Cancer Immunology and AIDS</addr-line>,<institution>Dana Farber Cancer Institute</institution></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af3"><addr-line>Department of Medicine</addr-line>,<institution>Harvard Medical School</institution>,<addr-line>Boston, MA 02115</addr-line>,<country>USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Gershoni, Jonathan M" sort="Gershoni, Jonathan M" uniqKey="Gershoni J" first="Jonathan M." last="Gershoni">Jonathan M. Gershoni</name><affiliation wicri:level="1"><nlm:aff id="af1"><addr-line>Department of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences</addr-line>,<institution>Tel Aviv University</institution>,<addr-line>Tel Aviv 69978</addr-line>,<country>Israel</country></nlm:aff><country xml:lang="fr">Israël</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Protein Engineering, Design and Selection</title><idno type="ISSN">1741-0126</idno><idno type="eISSN">1741-0134</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (genetics)</term><term>Amino Acid Sequence</term><term>Binding Sites (genetics)</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (genetics)</term><term>Peptide Fragments (metabolism)</term><term>Peptide Library</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>SARS Virus (genetics)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Banque de peptides</term><term>Données de séquences moléculaires</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (génétique)</term><term>Fragments peptidiques (métabolisme)</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (génétique)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés (génétique)</term><term>Peptidyl-Dipeptidase A ()</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Sites de fixation (génétique)</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Fragments</term><term>Peptidyl-Dipeptidase A</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Motifs</term><term>Binding Sites</term><term>Peptide Fragments</term><term>SARS Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Fragments peptidiques</term><term>Glycoprotéine de spicule des coronavirus</term><term>Motifs d'acides aminés</term><term>Sites de fixation</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Fragments</term><term>Peptidyl-Dipeptidase A</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fragments peptidiques</term><term>Glycoprotéine de spicule des coronavirus</term><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptide Library</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Banque de peptides</term><term>Données de séquences moléculaires</term><term>Fragments peptidiques</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>The severe acute respiratory syndrome (SARS) coronavirus (CoV) identified in 2003 has infected ∼8000 people worldwide, killing nearly 10% of them. The infection of target cells by the SARS CoV is mediated through the interaction of the viral Spike (S) protein (1255 amino acids) and its cellular receptor, angiotensin-converting enzyme 2 (ACE2). The SARS CoV receptor-binding domain (amino acids N318–T509 of S protein) harbors an extended excursion along its periphery that contacts ACE2 and is designated the receptor-binding motif (RBM, amino acids S432–T486). In addition, the RBM is a major antigenic determinant, able to elicit production of neutralizing antibodies. Hence, the role of the RBM is a bi-functional bioactive surface that can be demonstrated by antibodies such as the neutralizing human anti-SARS monoclonal antibody (mAb) 80R which targets the RBM and competes with the ACE2 receptor for binding. Here, we employ phage-display peptide-libraries to reconstitute a functional RBM. This is achieved by generating a vast collection of candidate RBM peptides that present a diversity of conformations. Screening such ‘Conformer Libraries’ with corresponding ligands has produced short RBM constructs (ca. 40 amino acids) that can bind both the ACE2 receptor and the neutralizing mAb 80R.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Babcock, G J" uniqKey="Babcock G">G.J. Babcock</name></author><author><name sortKey="Esshaki, D J" uniqKey="Esshaki D">D.J. Esshaki</name></author><author><name sortKey="Thomas, W D" uniqKey="Thomas W">W.D. Thomas</name></author><author><name sortKey="Ambrosino, D M" uniqKey="Ambrosino D">D.M. Ambrosino</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bailey, T L" uniqKey="Bailey T">T.L. Bailey</name></author><author><name sortKey="Boden, M" uniqKey="Boden M">M. Boden</name></author><author><name sortKey="Buske, F A" uniqKey="Buske F">F.A. Buske</name></author><author><name sortKey="Frith, M" uniqKey="Frith M">M. 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He</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Israël</li><li>République populaire de Chine</li><li>États-Unis</li></country></list><tree><country name="Israël"><noRegion><name sortKey="Freund, Natalia T" sort="Freund, Natalia T" uniqKey="Freund N" first="Natalia T." last="Freund">Natalia T. Freund</name></noRegion><name sortKey="Gershoni, Jonathan M" sort="Gershoni, Jonathan M" uniqKey="Gershoni J" first="Jonathan M." last="Gershoni">Jonathan M. Gershoni</name><name sortKey="Roitburd Berman, Anna" sort="Roitburd Berman, Anna" uniqKey="Roitburd Berman A" first="Anna" last="Roitburd-Berman">Anna Roitburd-Berman</name></country><country name="États-Unis"><noRegion><name sortKey="Freund, Natalia T" sort="Freund, Natalia T" uniqKey="Freund N" first="Natalia T." last="Freund">Natalia T. Freund</name></noRegion><name sortKey="Marasco, Wayne A" sort="Marasco, Wayne A" uniqKey="Marasco W" first="Wayne A." last="Marasco">Wayne A. Marasco</name><name sortKey="Sui, Jianhua" sort="Sui, Jianhua" uniqKey="Sui J" first="Jianhua" last="Sui">Jianhua Sui</name></country><country name="République populaire de Chine"><noRegion><name sortKey="Sui, Jianhua" sort="Sui, Jianhua" uniqKey="Sui J" first="Jianhua" last="Sui">Jianhua Sui</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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