SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway.
Identifieur interne : 001C27 ( PubMed/Corpus ); précédent : 001C26; suivant : 001C28SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway.
Auteurs : Hongliang Wang ; Peng Yang ; Kangtai Liu ; Feng Guo ; Yanli Zhang ; Gongyi Zhang ; Chengyu JiangSource :
- Cell research [ 1748-7838 ] ; 2008.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing, Calcium-Binding Proteins (genetics), Calcium-Binding Proteins (metabolism), Caveolae (metabolism), Caveolae (virology), Caveolin 1 (genetics), Caveolin 1 (metabolism), Cell Line, Clathrin (genetics), Clathrin (metabolism), Endocytosis (genetics), Endosomes (metabolism), Endosomes (virology), Humans, Hydrogen-Ion Concentration, Intracellular Signaling Peptides and Proteins (genetics), Intracellular Signaling Peptides and Proteins (metabolism), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (metabolism), Phosphoproteins (genetics), Phosphoproteins (metabolism), Protein Transport, SARS Virus (genetics), SARS Virus (metabolism), SARS Virus (pathogenicity), Severe Acute Respiratory Syndrome (drug therapy), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , genetics : Calcium-Binding Proteins, Caveolin 1, Clathrin, Intracellular Signaling Peptides and Proteins, Membrane Glycoproteins, Peptidyl-Dipeptidase A, Phosphoproteins, Viral Envelope Proteins.
- chemical , metabolism : Calcium-Binding Proteins, Caveolin 1, Clathrin, Intracellular Signaling Peptides and Proteins, Membrane Glycoproteins, Peptidyl-Dipeptidase A, Phosphoproteins, Viral Envelope Proteins.
- chemical : Adaptor Proteins, Signal Transducing, Spike Glycoprotein, Coronavirus.
- drug therapy : Severe Acute Respiratory Syndrome.
- genetics : Endocytosis, SARS Virus, Severe Acute Respiratory Syndrome.
- metabolism : Caveolae, Endosomes, SARS Virus, Severe Acute Respiratory Syndrome.
- pathogenicity : SARS Virus.
- virology : Caveolae, Endosomes.
- Cell Line, Humans, Hydrogen-Ion Concentration, Protein Transport, Virus Internalization.
Abstract
While severe acute respiratory syndrome coronavirus (SARS-CoV) was initially thought to enter cells through direct fusion with the plasma membrane, more recent evidence suggests that virus entry may also involve endocytosis. We have found that SARS-CoV enters cells via pH- and receptor-dependent endocytosis. Treatment of cells with either SARS-CoV spike protein or spike-bearing pseudoviruses resulted in the translocation of angiotensin-converting enzyme 2 (ACE2), the functional receptor of SARS-CoV, from the cell surface to endosomes. In addition, the spike-bearing pseudoviruses and early endosome antigen 1 were found to colocalize in endosomes. Further analyses using specific endocytic pathway inhibitors and dominant-negative Eps15 as well as caveolin-1 colocalization study suggested that virus entry was mediated by a clathrin- and caveolae-independent mechanism. Moreover, cholesterol- and sphingolipid-rich lipid raft microdomains in the plasma membrane, which have been shown to act as platforms for many physiological signaling pathways, were shown to be involved in virus entry. Endocytic entry of SARS-CoV may expand the cellular range of SARS-CoV infection, and our findings here contribute to the understanding of SARS-CoV pathogenesis, providing new information for anti-viral drug research.
DOI: 10.1038/cr.2008.15
PubMed: 18227861
Links to Exploration step
pubmed:18227861Le document en format XML
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first="Hongliang" last="Wang">Hongliang Wang</name><affiliation><nlm:affiliation>National Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Peking Union Medical College, Tsinghua University and Chinese Academy of Medical Sciences, Beijing 100005, China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Peng" sort="Yang, Peng" uniqKey="Yang P" first="Peng" last="Yang">Peng Yang</name></author><author><name sortKey="Liu, Kangtai" sort="Liu, Kangtai" uniqKey="Liu K" first="Kangtai" last="Liu">Kangtai Liu</name></author><author><name sortKey="Guo, Feng" sort="Guo, Feng" uniqKey="Guo F" first="Feng" last="Guo">Feng Guo</name></author><author><name sortKey="Zhang, Yanli" sort="Zhang, Yanli" uniqKey="Zhang Y" first="Yanli" last="Zhang">Yanli Zhang</name></author><author><name sortKey="Zhang, Gongyi" sort="Zhang, Gongyi" uniqKey="Zhang G" first="Gongyi" last="Zhang">Gongyi Zhang</name></author><author><name sortKey="Jiang, Chengyu" sort="Jiang, Chengyu" uniqKey="Jiang C" first="Chengyu" last="Jiang">Chengyu Jiang</name></author></analytic><series><title level="j">Cell research</title><idno type="eISSN">1748-7838</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Calcium-Binding Proteins (genetics)</term><term>Calcium-Binding Proteins (metabolism)</term><term>Caveolae (metabolism)</term><term>Caveolae (virology)</term><term>Caveolin 1 (genetics)</term><term>Caveolin 1 (metabolism)</term><term>Cell Line</term><term>Clathrin (genetics)</term><term>Clathrin (metabolism)</term><term>Endocytosis (genetics)</term><term>Endosomes (metabolism)</term><term>Endosomes (virology)</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Intracellular Signaling Peptides and Proteins (genetics)</term><term>Intracellular Signaling Peptides and Proteins (metabolism)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Peptidyl-Dipeptidase A (genetics)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Phosphoproteins (genetics)</term><term>Phosphoproteins (metabolism)</term><term>Protein Transport</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (pathogenicity)</term><term>Severe Acute Respiratory Syndrome (drug therapy)</term><term>Severe Acute Respiratory Syndrome (genetics)</term><term>Severe Acute Respiratory Syndrome (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Calcium-Binding Proteins</term><term>Caveolin 1</term><term>Clathrin</term><term>Intracellular Signaling Peptides and Proteins</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Phosphoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium-Binding Proteins</term><term>Caveolin 1</term><term>Clathrin</term><term>Intracellular Signaling Peptides and Proteins</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Phosphoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Endocytosis</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Caveolae</term><term>Endosomes</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Caveolae</term><term>Endosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Protein Transport</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">While severe acute respiratory syndrome coronavirus (SARS-CoV) was initially thought to enter cells through direct fusion with the plasma membrane, more recent evidence suggests that virus entry may also involve endocytosis. We have found that SARS-CoV enters cells via pH- and receptor-dependent endocytosis. Treatment of cells with either SARS-CoV spike protein or spike-bearing pseudoviruses resulted in the translocation of angiotensin-converting enzyme 2 (ACE2), the functional receptor of SARS-CoV, from the cell surface to endosomes. In addition, the spike-bearing pseudoviruses and early endosome antigen 1 were found to colocalize in endosomes. Further analyses using specific endocytic pathway inhibitors and dominant-negative Eps15 as well as caveolin-1 colocalization study suggested that virus entry was mediated by a clathrin- and caveolae-independent mechanism. Moreover, cholesterol- and sphingolipid-rich lipid raft microdomains in the plasma membrane, which have been shown to act as platforms for many physiological signaling pathways, were shown to be involved in virus entry. Endocytic entry of SARS-CoV may expand the cellular range of SARS-CoV infection, and our findings here contribute to the understanding of SARS-CoV pathogenesis, providing new information for anti-viral drug research.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18227861</PMID><DateCompleted><Year>2008</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1748-7838</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Cell research</Title><ISOAbbreviation>Cell Res.</ISOAbbreviation></Journal><ArticleTitle>SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway.</ArticleTitle><Pagination><MedlinePgn>290-301</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/cr.2008.15</ELocationID><Abstract><AbstractText>While severe acute respiratory syndrome coronavirus (SARS-CoV) was initially thought to enter cells through direct fusion with the plasma membrane, more recent evidence suggests that virus entry may also involve endocytosis. We have found that SARS-CoV enters cells via pH- and receptor-dependent endocytosis. Treatment of cells with either SARS-CoV spike protein or spike-bearing pseudoviruses resulted in the translocation of angiotensin-converting enzyme 2 (ACE2), the functional receptor of SARS-CoV, from the cell surface to endosomes. In addition, the spike-bearing pseudoviruses and early endosome antigen 1 were found to colocalize in endosomes. Further analyses using specific endocytic pathway inhibitors and dominant-negative Eps15 as well as caveolin-1 colocalization study suggested that virus entry was mediated by a clathrin- and caveolae-independent mechanism. Moreover, cholesterol- and sphingolipid-rich lipid raft microdomains in the plasma membrane, which have been shown to act as platforms for many physiological signaling pathways, were shown to be involved in virus entry. Endocytic entry of SARS-CoV may expand the cellular range of SARS-CoV infection, and our findings here contribute to the understanding of SARS-CoV pathogenesis, providing new information for anti-viral drug research.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Hongliang</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>National Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Peking Union Medical College, Tsinghua University and Chinese Academy of Medical Sciences, Beijing 100005, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Peng</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Kangtai</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Feng</ForeName><Initials>F</Initials></Author><Author 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