Highly conserved regions within the spike proteins of human coronaviruses 229E and NL63 determine recognition of their respective cellular receptors.
Identifieur interne : 003E79 ( Main/Exploration ); précédent : 003E78; suivant : 003E80Highly conserved regions within the spike proteins of human coronaviruses 229E and NL63 determine recognition of their respective cellular receptors.
Auteurs : Heike Hofmann [Allemagne] ; Graham Simmons ; Andrew J. Rennekamp ; Chawaree Chaipan ; Thomas Gramberg ; Elke Heck ; Martina Geier ; Anja Wegele ; Andrea Marzi ; Paul Bates ; Stefan PöhlmannSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Coronavirus (métabolisme), Coronavirus (pathogénicité), Coronavirus (physiologie), Coronavirus humain 229E (métabolisme), Coronavirus humain 229E (pathogénicité), Coronavirus humain 229E (physiologie), Cricetinae, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Lectines de type C (métabolisme), Lignée cellulaire, Molécules d'adhérence cellulaire (métabolisme), Peptidyl-Dipeptidase A (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Récepteurs de surface cellulaire (métabolisme), Récepteurs viraux (métabolisme), Souris.
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- métabolisme : Coronavirus, Coronavirus humain 229E, Glycoprotéines membranaires, Lectines de type C, Molécules d'adhérence cellulaire, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Récepteurs de surface cellulaire, Récepteurs viraux.
- pathogénicité : Coronavirus, Coronavirus humain 229E.
- physiologie : Coronavirus, Coronavirus humain 229E.
- Animaux, Cricetinae, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Lignée cellulaire, Protéines de l'enveloppe virale, Souris.
English descriptors
- KwdEn :
- Animals, Cell Adhesion Molecules (metabolism), Cell Line, Coronavirus (metabolism), Coronavirus (pathogenicity), Coronavirus (physiology), Coronavirus 229E, Human (metabolism), Coronavirus 229E, Human (pathogenicity), Coronavirus 229E, Human (physiology), Cricetinae, Humans, Lectins, C-Type (metabolism), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Peptidyl-Dipeptidase A (metabolism), Receptors, Cell Surface (metabolism), Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Cell Adhesion Molecules, Lectins, C-Type, Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Cell Surface, Receptors, Virus, Viral Envelope Proteins.
- metabolism : Coronavirus, Coronavirus 229E, Human.
- pathogenicity : Coronavirus, Coronavirus 229E, Human.
- physiology : Coronavirus, Coronavirus 229E, Human.
- Animals, Cell Line, Cricetinae, Humans, Mice, Spike Glycoprotein, Coronavirus.
Abstract
We have recently demonstrated that the severe acute respiratory syndrome coronavirus (SARS-CoV) receptor angiotensin converting enzyme 2 (ACE2) also mediates cellular entry of the newly discovered human coronavirus (hCoV) NL63. Here, we show that expression of DC-SIGN augments NL63 spike (S)-protein-driven infection of susceptible cells, while only expression of ACE2 but not DC-SIGN is sufficient for entry into nonpermissive cells, indicating that ACE2 fulfills the criteria of a bona fide hCoV-NL63 receptor. As for SARS-CoV, murine ACE2 is used less efficiently by NL63-S for entry than human ACE2. In contrast, several amino acid exchanges in human ACE2 which diminish SARS-S-driven entry do not interfere with NL63-S-mediated infection, suggesting that SARS-S and NL63-S might engage human ACE2 differentially. Moreover, we observed that NL63-S-driven entry was less dependent on a low-pH environment and activity of endosomal proteases compared to infection mediated by SARS-S, further suggesting differences in hCoV-NL63 and SARS-CoV cellular entry. NL63-S does not exhibit significant homology to SARS-S but is highly related to the S-protein of hCoV-229E, which enters target cells by engaging CD13. Employing mutagenic analyses, we found that the N-terminal unique domain in NL63-S, which is absent in 229E-S, does not confer binding to ACE2. In contrast, the highly homologous C-terminal parts of the NL63-S1 and 229E-S1 subunits in conjunction with distinct amino acids in the central regions of these proteins confer recognition of ACE2 and CD13, respectively. Therefore, despite the high homology of these sequences, they likely form sufficiently distinct surfaces, thus determining receptor specificity.
DOI: 10.1128/JVI.00560-06
PubMed: 16912312
Affiliations:
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Rennekamp</name></author><author><name sortKey="Chaipan, Chawaree" sort="Chaipan, Chawaree" uniqKey="Chaipan C" first="Chawaree" last="Chaipan">Chawaree Chaipan</name></author><author><name sortKey="Gramberg, Thomas" sort="Gramberg, Thomas" uniqKey="Gramberg T" first="Thomas" last="Gramberg">Thomas Gramberg</name></author><author><name sortKey="Heck, Elke" sort="Heck, Elke" uniqKey="Heck E" first="Elke" last="Heck">Elke Heck</name></author><author><name sortKey="Geier, Martina" sort="Geier, Martina" uniqKey="Geier M" first="Martina" last="Geier">Martina Geier</name></author><author><name sortKey="Wegele, Anja" sort="Wegele, Anja" uniqKey="Wegele A" first="Anja" last="Wegele">Anja Wegele</name></author><author><name sortKey="Marzi, Andrea" sort="Marzi, Andrea" uniqKey="Marzi A" first="Andrea" last="Marzi">Andrea Marzi</name></author><author><name sortKey="Bates, Paul" sort="Bates, Paul" uniqKey="Bates P" first="Paul" last="Bates">Paul Bates</name></author><author><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Adhesion Molecules (metabolism)</term><term>Cell Line</term><term>Coronavirus (metabolism)</term><term>Coronavirus (pathogenicity)</term><term>Coronavirus (physiology)</term><term>Coronavirus 229E, Human (metabolism)</term><term>Coronavirus 229E, Human (pathogenicity)</term><term>Coronavirus 229E, Human (physiology)</term><term>Cricetinae</term><term>Humans</term><term>Lectins, C-Type (metabolism)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Receptors, Cell Surface (metabolism)</term><term>Receptors, Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Coronavirus (métabolisme)</term><term>Coronavirus (pathogénicité)</term><term>Coronavirus (physiologie)</term><term>Coronavirus humain 229E (métabolisme)</term><term>Coronavirus humain 229E (pathogénicité)</term><term>Coronavirus humain 229E (physiologie)</term><term>Cricetinae</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Lectines de type C (métabolisme)</term><term>Lignée cellulaire</term><term>Molécules d'adhérence cellulaire (métabolisme)</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Récepteurs de surface cellulaire (métabolisme)</term><term>Récepteurs viraux (métabolisme)</term><term>Souris</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cell Adhesion Molecules</term><term>Lectins, C-Type</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Cell Surface</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term><term>Coronavirus 229E, Human</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term><term>Coronavirus humain 229E</term><term>Glycoprotéines membranaires</term><term>Lectines de type C</term><term>Molécules d'adhérence cellulaire</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs de surface cellulaire</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Coronavirus</term><term>Coronavirus 229E, Human</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Coronavirus</term><term>Coronavirus humain 229E</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term><term>Coronavirus humain 229E</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term><term>Coronavirus 229E, Human</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cricetinae</term><term>Humans</term><term>Mice</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cricetinae</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have recently demonstrated that the severe acute respiratory syndrome coronavirus (SARS-CoV) receptor angiotensin converting enzyme 2 (ACE2) also mediates cellular entry of the newly discovered human coronavirus (hCoV) NL63. Here, we show that expression of DC-SIGN augments NL63 spike (S)-protein-driven infection of susceptible cells, while only expression of ACE2 but not DC-SIGN is sufficient for entry into nonpermissive cells, indicating that ACE2 fulfills the criteria of a bona fide hCoV-NL63 receptor. As for SARS-CoV, murine ACE2 is used less efficiently by NL63-S for entry than human ACE2. In contrast, several amino acid exchanges in human ACE2 which diminish SARS-S-driven entry do not interfere with NL63-S-mediated infection, suggesting that SARS-S and NL63-S might engage human ACE2 differentially. Moreover, we observed that NL63-S-driven entry was less dependent on a low-pH environment and activity of endosomal proteases compared to infection mediated by SARS-S, further suggesting differences in hCoV-NL63 and SARS-CoV cellular entry. NL63-S does not exhibit significant homology to SARS-S but is highly related to the S-protein of hCoV-229E, which enters target cells by engaging CD13. Employing mutagenic analyses, we found that the N-terminal unique domain in NL63-S, which is absent in 229E-S, does not confer binding to ACE2. In contrast, the highly homologous C-terminal parts of the NL63-S1 and 229E-S1 subunits in conjunction with distinct amino acids in the central regions of these proteins confer recognition of ACE2 and CD13, respectively. Therefore, despite the high homology of these sequences, they likely form sufficiently distinct surfaces, thus determining receptor specificity.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Bates, Paul" sort="Bates, Paul" uniqKey="Bates P" first="Paul" last="Bates">Paul Bates</name><name sortKey="Chaipan, Chawaree" sort="Chaipan, Chawaree" uniqKey="Chaipan C" first="Chawaree" last="Chaipan">Chawaree Chaipan</name><name sortKey="Geier, Martina" sort="Geier, Martina" uniqKey="Geier M" first="Martina" last="Geier">Martina Geier</name><name sortKey="Gramberg, Thomas" sort="Gramberg, Thomas" uniqKey="Gramberg T" first="Thomas" last="Gramberg">Thomas Gramberg</name><name sortKey="Heck, Elke" sort="Heck, Elke" uniqKey="Heck E" first="Elke" last="Heck">Elke Heck</name><name sortKey="Marzi, Andrea" sort="Marzi, Andrea" uniqKey="Marzi A" first="Andrea" last="Marzi">Andrea Marzi</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><name sortKey="Rennekamp, Andrew J" sort="Rennekamp, Andrew J" uniqKey="Rennekamp A" first="Andrew J" last="Rennekamp">Andrew J. Rennekamp</name><name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name><name sortKey="Wegele, Anja" sort="Wegele, Anja" uniqKey="Wegele A" first="Anja" last="Wegele">Anja Wegele</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Hofmann, Heike" sort="Hofmann, Heike" uniqKey="Hofmann H" first="Heike" last="Hofmann">Heike Hofmann</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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