Inhibition of endoplasmic reticulum-resident glucosidases impairs severe acute respiratory syndrome coronavirus and human coronavirus NL63 spike protein-mediated entry by altering the glycan processing of angiotensin I-converting enzyme 2.
Identifieur interne : 000F11 ( PubMed/Curation ); précédent : 000F10; suivant : 000F12Inhibition of endoplasmic reticulum-resident glucosidases impairs severe acute respiratory syndrome coronavirus and human coronavirus NL63 spike protein-mediated entry by altering the glycan processing of angiotensin I-converting enzyme 2.
Auteurs : Xuesen Zhao [États-Unis] ; Fang Guo [États-Unis] ; Mary Ann Comunale [États-Unis] ; Anand Mehta [États-Unis] ; Mohit Sehgal [États-Unis] ; Pooja Jain [États-Unis] ; Andrea Cuconati [États-Unis] ; Hanxin Lin [Canada] ; Timothy M. Block [États-Unis] ; Jinhong Chang [États-Unis] ; Ju-Tao Guo [États-Unis]Source :
- Antimicrobial agents and chemotherapy [ 1098-6596 ] ; 2015.
Descripteurs français
- KwdFr :
- Antienzymes (), Antienzymes (métabolisme), Antienzymes (pharmacologie), Antiviraux (), Antiviraux (pharmacologie), Coronavirus humain NL63 (), Coronavirus humain NL63 (pathogénicité), Glucosidases (antagonistes et inhibiteurs), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Iminosucres (), Iminosucres (pharmacologie), Interactions hôte-pathogène (), Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (métabolisme), Pénétration virale (), Réticulum endoplasmique (), Réticulum endoplasmique (métabolisme), Thérapie moléculaire ciblée, Virus du SRAS (), Virus du SRAS (pathogénicité).
- MESH :
- antagonistes et inhibiteurs : Glucosidases.
- métabolisme : Antienzymes, Glycoprotéine de spicule des coronavirus, Peptidyl-Dipeptidase A, Réticulum endoplasmique.
- pathogénicité : Coronavirus humain NL63, Virus du SRAS.
- pharmacologie : Antienzymes, Antiviraux, Iminosucres.
- Antienzymes, Antiviraux, Coronavirus humain NL63, Humains, Iminosucres, Interactions hôte-pathogène, Peptidyl-Dipeptidase A, Pénétration virale, Réticulum endoplasmique, Thérapie moléculaire ciblée, Virus du SRAS.
English descriptors
- KwdEn :
- Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Coronavirus NL63, Human (drug effects), Coronavirus NL63, Human (pathogenicity), Endoplasmic Reticulum (drug effects), Endoplasmic Reticulum (metabolism), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (metabolism), Enzyme Inhibitors (pharmacology), Glucosidases (antagonists & inhibitors), Host-Pathogen Interactions (drug effects), Humans, Imino Sugars (chemistry), Imino Sugars (pharmacology), Molecular Targeted Therapy, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (metabolism), SARS Virus (drug effects), SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization (drug effects).
- MESH :
- chemical , antagonists & inhibitors : Glucosidases.
- chemical , chemistry : Antiviral Agents, Enzyme Inhibitors, Imino Sugars, Peptidyl-Dipeptidase A.
- chemical , metabolism : Enzyme Inhibitors, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus.
- chemical , pharmacology : Antiviral Agents, Enzyme Inhibitors, Imino Sugars.
- drug effects : Coronavirus NL63, Human, Endoplasmic Reticulum, Host-Pathogen Interactions, SARS Virus, Virus Internalization.
- metabolism : Endoplasmic Reticulum.
- pathogenicity : Coronavirus NL63, Human, SARS Virus.
- Humans, Molecular Targeted Therapy.
Abstract
Endoplasmic reticulum (ER)-resident glucosidases I and II sequentially trim the three terminal glucose moieties on the N-linked glycans attached to nascent glycoproteins. These reactions are the first steps of N-linked glycan processing and are essential for proper folding and function of many glycoproteins. Because most of the viral envelope glycoproteins contain N-linked glycans, inhibition of ER glucosidases with derivatives of 1-deoxynojirimycin, i.e., iminosugars, efficiently disrupts the morphogenesis of a broad spectrum of enveloped viruses. However, like viral envelope proteins, the cellular receptors of many viruses are also glycoproteins. It is therefore possible that inhibition of ER glucosidases not only compromises virion production but also disrupts expression and function of viral receptors and thus inhibits virus entry into host cells. Indeed, we demonstrate here that iminosugar treatment altered the N-linked glycan structure of angiotensin I-converting enzyme 2 (ACE2), which did not affect its expression on the cell surface or its binding of the severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein. However, alteration of N-linked glycans of ACE2 impaired its ability to support the transduction of SARS-CoV and human coronavirus NL63 (HCoV-NL63) spike glycoprotein-pseudotyped lentiviral particles by disruption of the viral envelope protein-triggered membrane fusion. Hence, in addition to reducing the production of infectious virions, inhibition of ER glucosidases also impairs the entry of selected viruses via a post-receptor-binding mechanism.
DOI: 10.1128/AAC.03999-14
PubMed: 25348530
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Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Lin, Hanxin" sort="Lin, Hanxin" uniqKey="Lin H" first="Hanxin" last="Lin">Hanxin Lin</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pathology and Molecular Medicine, McMaster University, Hamilton</wicri:regionArea></affiliation></author><author><name sortKey="Block, Timothy M" sort="Block, Timothy M" uniqKey="Block T" first="Timothy M" last="Block">Timothy M. Block</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Chang, Jinhong" sort="Chang, Jinhong" uniqKey="Chang J" first="Jinhong" last="Chang">Jinhong Chang</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Guo, Ju Tao" sort="Guo, Ju Tao" uniqKey="Guo J" first="Ju-Tao" last="Guo">Ju-Tao Guo</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Ju-Tao.Guo@drexelmed.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25348530</idno><idno type="pmid">25348530</idno><idno type="doi">10.1128/AAC.03999-14</idno><idno type="wicri:Area/PubMed/Corpus">000F11</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000F11</idno><idno type="wicri:Area/PubMed/Curation">000F11</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000F11</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibition of endoplasmic reticulum-resident glucosidases impairs severe acute respiratory syndrome coronavirus and human coronavirus NL63 spike protein-mediated entry by altering the glycan processing of angiotensin I-converting enzyme 2.</title><author><name sortKey="Zhao, Xuesen" sort="Zhao, Xuesen" uniqKey="Zhao X" first="Xuesen" last="Zhao">Xuesen Zhao</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Guo, Fang" sort="Guo, Fang" uniqKey="Guo F" first="Fang" last="Guo">Fang Guo</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Comunale, Mary Ann" sort="Comunale, Mary Ann" uniqKey="Comunale M" first="Mary Ann" last="Comunale">Mary Ann Comunale</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Mehta, Anand" sort="Mehta, Anand" uniqKey="Mehta A" first="Anand" last="Mehta">Anand Mehta</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Sehgal, Mohit" sort="Sehgal, Mohit" uniqKey="Sehgal M" first="Mohit" last="Sehgal">Mohit Sehgal</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Jain, Pooja" sort="Jain, Pooja" uniqKey="Jain P" first="Pooja" last="Jain">Pooja Jain</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Cuconati, Andrea" sort="Cuconati, Andrea" uniqKey="Cuconati A" first="Andrea" last="Cuconati">Andrea Cuconati</name><affiliation wicri:level="1"><nlm:affiliation>Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Lin, Hanxin" sort="Lin, Hanxin" uniqKey="Lin H" first="Hanxin" last="Lin">Hanxin Lin</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pathology and Molecular Medicine, McMaster University, Hamilton</wicri:regionArea></affiliation></author><author><name sortKey="Block, Timothy M" sort="Block, Timothy M" uniqKey="Block T" first="Timothy M" last="Block">Timothy M. Block</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Chang, Jinhong" sort="Chang, Jinhong" uniqKey="Chang J" first="Jinhong" last="Chang">Jinhong Chang</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Guo, Ju Tao" sort="Guo, Ju Tao" uniqKey="Guo J" first="Ju-Tao" last="Guo">Ju-Tao Guo</name><affiliation wicri:level="1"><nlm:affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Ju-Tao.Guo@drexelmed.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania</wicri:regionArea></affiliation></author></analytic><series><title level="j">Antimicrobial agents and chemotherapy</title><idno type="eISSN">1098-6596</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (chemistry)</term><term>Antiviral Agents (pharmacology)</term><term>Coronavirus NL63, Human (drug effects)</term><term>Coronavirus NL63, Human (pathogenicity)</term><term>Endoplasmic Reticulum (drug effects)</term><term>Endoplasmic Reticulum (metabolism)</term><term>Enzyme Inhibitors (chemistry)</term><term>Enzyme Inhibitors (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Glucosidases (antagonists & inhibitors)</term><term>Host-Pathogen Interactions (drug effects)</term><term>Humans</term><term>Imino Sugars (chemistry)</term><term>Imino Sugars (pharmacology)</term><term>Molecular Targeted Therapy</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (pathogenicity)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Virus Internalization (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes ()</term><term>Antienzymes (métabolisme)</term><term>Antienzymes (pharmacologie)</term><term>Antiviraux ()</term><term>Antiviraux (pharmacologie)</term><term>Coronavirus humain NL63 ()</term><term>Coronavirus humain NL63 (pathogénicité)</term><term>Glucosidases (antagonistes et inhibiteurs)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Iminosucres ()</term><term>Iminosucres (pharmacologie)</term><term>Interactions hôte-pathogène ()</term><term>Peptidyl-Dipeptidase A ()</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Pénétration virale ()</term><term>Réticulum endoplasmique ()</term><term>Réticulum endoplasmique (métabolisme)</term><term>Thérapie moléculaire ciblée</term><term>Virus du SRAS ()</term><term>Virus du SRAS (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Glucosidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term><term>Enzyme Inhibitors</term><term>Imino Sugars</term><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzyme Inhibitors</term><term>Peptidyl-Dipeptidase A</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Enzyme Inhibitors</term><term>Imino Sugars</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Glucosidases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Coronavirus NL63, Human</term><term>Endoplasmic Reticulum</term><term>Host-Pathogen Interactions</term><term>SARS Virus</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endoplasmic Reticulum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antienzymes</term><term>Glycoprotéine de spicule des coronavirus</term><term>Peptidyl-Dipeptidase A</term><term>Réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Coronavirus NL63, Human</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Coronavirus humain NL63</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term><term>Antiviraux</term><term>Iminosucres</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Molecular Targeted Therapy</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Antienzymes</term><term>Antiviraux</term><term>Coronavirus humain NL63</term><term>Humains</term><term>Iminosucres</term><term>Interactions hôte-pathogène</term><term>Peptidyl-Dipeptidase A</term><term>Pénétration virale</term><term>Réticulum endoplasmique</term><term>Thérapie moléculaire ciblée</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Endoplasmic reticulum (ER)-resident glucosidases I and II sequentially trim the three terminal glucose moieties on the N-linked glycans attached to nascent glycoproteins. These reactions are the first steps of N-linked glycan processing and are essential for proper folding and function of many glycoproteins. Because most of the viral envelope glycoproteins contain N-linked glycans, inhibition of ER glucosidases with derivatives of 1-deoxynojirimycin, i.e., iminosugars, efficiently disrupts the morphogenesis of a broad spectrum of enveloped viruses. However, like viral envelope proteins, the cellular receptors of many viruses are also glycoproteins. It is therefore possible that inhibition of ER glucosidases not only compromises virion production but also disrupts expression and function of viral receptors and thus inhibits virus entry into host cells. Indeed, we demonstrate here that iminosugar treatment altered the N-linked glycan structure of angiotensin I-converting enzyme 2 (ACE2), which did not affect its expression on the cell surface or its binding of the severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein. However, alteration of N-linked glycans of ACE2 impaired its ability to support the transduction of SARS-CoV and human coronavirus NL63 (HCoV-NL63) spike glycoprotein-pseudotyped lentiviral particles by disruption of the viral envelope protein-triggered membrane fusion. Hence, in addition to reducing the production of infectious virions, inhibition of ER glucosidases also impairs the entry of selected viruses via a post-receptor-binding mechanism. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25348530</PMID><DateCompleted><Year>2016</Year><Month>05</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-6596</ISSN><JournalIssue CitedMedium="Internet"><Volume>59</Volume><Issue>1</Issue><PubDate><Year>2015</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Antimicrobial agents and chemotherapy</Title><ISOAbbreviation>Antimicrob. Agents Chemother.</ISOAbbreviation></Journal><ArticleTitle>Inhibition of endoplasmic reticulum-resident glucosidases impairs severe acute respiratory syndrome coronavirus and human coronavirus NL63 spike protein-mediated entry by altering the glycan processing of angiotensin I-converting enzyme 2.</ArticleTitle><Pagination><MedlinePgn>206-16</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AAC.03999-14</ELocationID><Abstract><AbstractText>Endoplasmic reticulum (ER)-resident glucosidases I and II sequentially trim the three terminal glucose moieties on the N-linked glycans attached to nascent glycoproteins. These reactions are the first steps of N-linked glycan processing and are essential for proper folding and function of many glycoproteins. Because most of the viral envelope glycoproteins contain N-linked glycans, inhibition of ER glucosidases with derivatives of 1-deoxynojirimycin, i.e., iminosugars, efficiently disrupts the morphogenesis of a broad spectrum of enveloped viruses. However, like viral envelope proteins, the cellular receptors of many viruses are also glycoproteins. It is therefore possible that inhibition of ER glucosidases not only compromises virion production but also disrupts expression and function of viral receptors and thus inhibits virus entry into host cells. Indeed, we demonstrate here that iminosugar treatment altered the N-linked glycan structure of angiotensin I-converting enzyme 2 (ACE2), which did not affect its expression on the cell surface or its binding of the severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein. However, alteration of N-linked glycans of ACE2 impaired its ability to support the transduction of SARS-CoV and human coronavirus NL63 (HCoV-NL63) spike glycoprotein-pseudotyped lentiviral particles by disruption of the viral envelope protein-triggered membrane fusion. Hence, in addition to reducing the production of infectious virions, inhibition of ER glucosidases also impairs the entry of selected viruses via a post-receptor-binding mechanism. </AbstractText><CopyrightInformation>Copyright © 2015, American Society for Microbiology. All Rights Reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Xuesen</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Fang</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Comunale</LastName><ForeName>Mary Ann</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mehta</LastName><ForeName>Anand</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sehgal</LastName><ForeName>Mohit</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jain</LastName><ForeName>Pooja</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cuconati</LastName><ForeName>Andrea</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Hanxin</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Pathology and Molecular Medicine, McMaster University, Hamilton, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Block</LastName><ForeName>Timothy M</ForeName><Initials>TM</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Baruch S. Blumberg Institute, Hepatitis B Foundation, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Jinhong</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Ju-Tao</ForeName><Initials>JT</Initials><AffiliationInfo><Affiliation>Drexel Institute for Biotechnology and Virology Research, Department of Microbiology and Immunology, Drexel University College of Medicine, Doylestown, Pennsylvania, USA Ju-Tao.Guo@drexelmed.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 CA054559</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U01 CA168856</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA120206</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI104636</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI104636</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antimicrob Agents Chemother</MedlineTA><NlmUniqueID>0315061</NlmUniqueID><ISSNLinking>0066-4804</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C585142">CM-10-18 compound</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000600715">IHVR-11029</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000600716">IHVR-17028</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050111">Imino Sugars</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578559">spike glycoprotein, human coronavirus (HCV)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D005959">Glucosidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058957" MajorTopicYN="N">Coronavirus NL63, Human</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005959" MajorTopicYN="N">Glucosidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050111" MajorTopicYN="N">Imino Sugars</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058990" MajorTopicYN="N">Molecular Targeted Therapy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug 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