Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain.
Identifieur interne : 002B97 ( PubMed/Corpus ); précédent : 002B96; suivant : 002B98Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain.
Auteurs : Rong Ye ; Cynthia Montalto-Morrison ; Paul S. MastersSource :
- Journal of virology [ 0022-538X ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cysteine (chemistry), DNA, Viral (genetics), Genes, Reporter, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Mice, Molecular Sequence Data, Murine hepatitis virus (genetics), Murine hepatitis virus (pathogenicity), Murine hepatitis virus (physiology), Protein Structure, Tertiary, Recombination, Genetic, Sequence Deletion, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Virus Assembly (genetics), Virus Assembly (physiology).
- MESH :
- chemical , chemistry : Cysteine, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : DNA, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : Murine hepatitis virus, Virus Assembly.
- pathogenicity : Murine hepatitis virus.
- physiology : Murine hepatitis virus, Virus Assembly.
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Genes, Reporter, Membrane Fusion, Mice, Molecular Sequence Data, Protein Structure, Tertiary, Recombination, Genetic, Sequence Deletion, Spike Glycoprotein, Coronavirus.
Abstract
The coronavirus spike protein (S) forms the distinctive virion surface structures that are characteristic of this viral family, appearing in negatively stained electron microscopy as stems capped with spherical bulbs. These structures are essential for the initiation of infection through attachment of the virus to cellular receptors followed by fusion to host cell membranes. The S protein can also mediate the formation of syncytia in infected cells. The S protein is a type I transmembrane protein that is very large compared to other viral fusion proteins, and all except a short carboxy-terminal segment of the S molecule constitutes the ectodomain. For the prototype coronavirus mouse hepatitis virus (MHV), it has previously been established that S protein assembly into virions is specified by the carboxy-terminal segment, which comprises the transmembrane domain and the endodomain. We have genetically dissected these domains in the MHV S protein to localize the determinants of S incorporation into virions. Our results establish that assembly competence maps to the endodomain of S, which was shown to be sufficient to target a heterologous integral membrane protein for incorporation into MHV virions. In particular, mutational analysis indicated a major role for the charge-rich carboxy-terminal region of the endodomain. Additionally, we found that the adjacent cysteine-rich region of the endodomain is critical for fusion of infected cells, confirming results previously obtained with S protein expression systems.
DOI: 10.1128/JVI.78.18.9904-9917.2004
PubMed: 15331724
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pubmed:15331724Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain.</title><author><name sortKey="Ye, Rong" sort="Ye, Rong" uniqKey="Ye R" first="Rong" last="Ye">Rong Ye</name><affiliation><nlm:affiliation>Wadsworth Center, New York State Department of Health, New Scotland Ave., P.O. Box 22002, Albany, NY 12201-2002, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Montalto Morrison, Cynthia" sort="Montalto Morrison, Cynthia" uniqKey="Montalto Morrison C" first="Cynthia" last="Montalto-Morrison">Cynthia Montalto-Morrison</name></author><author><name sortKey="Masters, Paul S" sort="Masters, Paul S" uniqKey="Masters P" first="Paul S" last="Masters">Paul S. Masters</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15331724</idno><idno type="pmid">15331724</idno><idno type="doi">10.1128/JVI.78.18.9904-9917.2004</idno><idno type="wicri:Area/PubMed/Corpus">002B97</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002B97</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain.</title><author><name sortKey="Ye, Rong" sort="Ye, Rong" uniqKey="Ye R" first="Rong" last="Ye">Rong Ye</name><affiliation><nlm:affiliation>Wadsworth Center, New York State Department of Health, New Scotland Ave., P.O. Box 22002, Albany, NY 12201-2002, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Montalto Morrison, Cynthia" sort="Montalto Morrison, Cynthia" uniqKey="Montalto Morrison C" first="Cynthia" last="Montalto-Morrison">Cynthia Montalto-Morrison</name></author><author><name sortKey="Masters, Paul S" sort="Masters, Paul S" uniqKey="Masters P" first="Paul S" last="Masters">Paul S. Masters</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cell Line</term><term>Cysteine (chemistry)</term><term>DNA, Viral (genetics)</term><term>Genes, Reporter</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Mice</term><term>Molecular Sequence Data</term><term>Murine hepatitis virus (genetics)</term><term>Murine hepatitis virus (pathogenicity)</term><term>Murine hepatitis virus (physiology)</term><term>Protein Structure, Tertiary</term><term>Recombination, Genetic</term><term>Sequence Deletion</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Virus Assembly (genetics)</term><term>Virus Assembly (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Viral</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cell Line</term><term>Genes, Reporter</term><term>Membrane Fusion</term><term>Mice</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Recombination, Genetic</term><term>Sequence Deletion</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus spike protein (S) forms the distinctive virion surface structures that are characteristic of this viral family, appearing in negatively stained electron microscopy as stems capped with spherical bulbs. These structures are essential for the initiation of infection through attachment of the virus to cellular receptors followed by fusion to host cell membranes. The S protein can also mediate the formation of syncytia in infected cells. The S protein is a type I transmembrane protein that is very large compared to other viral fusion proteins, and all except a short carboxy-terminal segment of the S molecule constitutes the ectodomain. For the prototype coronavirus mouse hepatitis virus (MHV), it has previously been established that S protein assembly into virions is specified by the carboxy-terminal segment, which comprises the transmembrane domain and the endodomain. We have genetically dissected these domains in the MHV S protein to localize the determinants of S incorporation into virions. Our results establish that assembly competence maps to the endodomain of S, which was shown to be sufficient to target a heterologous integral membrane protein for incorporation into MHV virions. In particular, mutational analysis indicated a major role for the charge-rich carboxy-terminal region of the endodomain. Additionally, we found that the adjacent cysteine-rich region of the endodomain is critical for fusion of infected cells, confirming results previously obtained with S protein expression systems.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15331724</PMID><DateCompleted><Year>2004</Year><Month>09</Month><Day>28</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>78</Volume><Issue>18</Issue><PubDate><Year>2004</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain.</ArticleTitle><Pagination><MedlinePgn>9904-17</MedlinePgn></Pagination><Abstract><AbstractText>The coronavirus spike protein (S) forms the distinctive virion surface structures that are characteristic of this viral family, appearing in negatively stained electron microscopy as stems capped with spherical bulbs. These structures are essential for the initiation of infection through attachment of the virus to cellular receptors followed by fusion to host cell membranes. The S protein can also mediate the formation of syncytia in infected cells. The S protein is a type I transmembrane protein that is very large compared to other viral fusion proteins, and all except a short carboxy-terminal segment of the S molecule constitutes the ectodomain. For the prototype coronavirus mouse hepatitis virus (MHV), it has previously been established that S protein assembly into virions is specified by the carboxy-terminal segment, which comprises the transmembrane domain and the endodomain. We have genetically dissected these domains in the MHV S protein to localize the determinants of S incorporation into virions. Our results establish that assembly competence maps to the endodomain of S, which was shown to be sufficient to target a heterologous integral membrane protein for incorporation into MHV virions. In particular, mutational analysis indicated a major role for the charge-rich carboxy-terminal region of the endodomain. Additionally, we found that the adjacent cysteine-rich region of the endodomain is critical for fusion of infected cells, confirming results previously obtained with S protein expression systems.</AbstractText><CopyrightInformation>Copyright 2004 American Society for Microbiology</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Rong</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Wadsworth Center, New York State Department of Health, New Scotland Ave., P.O. Box 22002, Albany, NY 12201-2002, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Montalto-Morrison</LastName><ForeName>Cynthia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Masters</LastName><ForeName>Paul S</ForeName><Initials>PS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI039544</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI045695</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI 39544</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI 45695</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004279">DNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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