Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA
Identifieur interne : 002592 ( Main/Exploration ); précédent : 002591; suivant : 002593Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA
Auteurs : Michael G. Roth [États-Unis] ; Richard W. Compans [États-Unis] ; Lorraine Giusti [États-Unis] ; Alan R. Davis [États-Unis] ; Debi P. Nayak [États-Unis] ; Mary-Jane Gething [États-Unis] ; Joe Sambrook [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1983.
English descriptors
- Teeft :
- Acad, Agmk, Agmk cell, Agmk cells, Apical, Apical surface, Apical surfaces, Basal, Basal membranes, Basal surface, Basal surfaces, Basolateral, Basolateral membranes, Boulan, Cell biol, Cell cultures, Cell surface, Compans, Epithelial, Epithelial cells, Ferritin, Ferritin conjugate, Gething, Glycoprotein, Hemagglutinin, Hemagglutinin gene, Influenza, Influenza virions, Influenza virus, Influenza virus glycoproteins, Influenza virus maturation, Influenza viruses, Klenk, Mdck, Mdck cells, Membrane, Membrane domain, Monkey kidney, Monolayers, Nonpolarized, Plasma membrane, Plastic dishes, Postinfection, Primary agmk cells, Recombinant, Rodriguez, Rodriguez boulan, Roth, Surface expression, Surface glycoproteins, Tight junctions, Vesicular stomatitis virus, Viral, Viral glycoproteins, Virion, Virus, Virus maturation.
Abstract
Abstract: Primary cell cultures of African Green monkey kidney (AGMK) contain polarized epithelial cells in which influenza virus matures predominantly at the apical surfaces above tight junctions. Influenza virus glycoproteins were found to be localized at the same membrane domain from which the virus budded. When polarized primary AGMK cells were infected with recombinant SV40 viruses containing DNA coding for either an influenza virus H1 or H2 subtype hemagglutinin (HA), the HA proteins were preferentially expressed at the apical surface in a manner identical to that observed in influenza virus-infected cells. Thus, cellular mechanisms for sorting membrane glycoproteins recognize some structural feature of the HA glycoprotein itself, and other viral proteins are not necessary for this process.
Url:
DOI: 10.1016/0092-8674(83)90425-7
Affiliations:
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Le document en format XML
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Compans</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Department of Microbiology University of Alabama in Birmingham Birmingham</wicri:cityArea></affiliation></author><author><name sortKey="Giusti, Lorraine" sort="Giusti, Lorraine" uniqKey="Giusti L" first="Lorraine" last="Giusti">Lorraine Giusti</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>University of California, Los Angeles Jonsson Comprehensive Cancer Center and Department of Microbiology and Immunology University of California, Los Angeles, School of Medicine, Los Angeles</wicri:cityArea></affiliation></author><author><name sortKey="Davis, Alan R" sort="Davis, Alan R" uniqKey="Davis A" first="Alan R." last="Davis">Alan R. Davis</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>University of California, Los Angeles Jonsson Comprehensive Cancer Center and Department of Microbiology and Immunology University of California, Los Angeles, School of Medicine, Los Angeles</wicri:cityArea></affiliation></author><author><name sortKey="Nayak, Debi P" sort="Nayak, Debi P" uniqKey="Nayak D" first="Debi P." last="Nayak">Debi P. Nayak</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>University of California, Los Angeles Jonsson Comprehensive Cancer Center and Department of Microbiology and Immunology University of California, Los Angeles, School of Medicine, Los Angeles</wicri:cityArea></affiliation></author><author><name sortKey="Gething, Mary Jane" sort="Gething, Mary Jane" uniqKey="Gething M" first="Mary-Jane" last="Gething">Mary-Jane Gething</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Cold Spring Harbor Laboratory Cold Spring Harbor</wicri:cityArea></affiliation></author><author><name sortKey="Sambrook, Joe" sort="Sambrook, Joe" uniqKey="Sambrook J" first="Joe" last="Sambrook">Joe Sambrook</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Cold Spring Harbor Laboratory Cold Spring Harbor</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1983">1983</date><biblScope unit="volume">33</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="435">435</biblScope><biblScope unit="page" to="443">443</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Agmk</term><term>Agmk cell</term><term>Agmk cells</term><term>Apical</term><term>Apical surface</term><term>Apical surfaces</term><term>Basal</term><term>Basal membranes</term><term>Basal surface</term><term>Basal surfaces</term><term>Basolateral</term><term>Basolateral membranes</term><term>Boulan</term><term>Cell biol</term><term>Cell cultures</term><term>Cell surface</term><term>Compans</term><term>Epithelial</term><term>Epithelial cells</term><term>Ferritin</term><term>Ferritin conjugate</term><term>Gething</term><term>Glycoprotein</term><term>Hemagglutinin</term><term>Hemagglutinin gene</term><term>Influenza</term><term>Influenza virions</term><term>Influenza virus</term><term>Influenza virus glycoproteins</term><term>Influenza virus maturation</term><term>Influenza viruses</term><term>Klenk</term><term>Mdck</term><term>Mdck cells</term><term>Membrane</term><term>Membrane domain</term><term>Monkey kidney</term><term>Monolayers</term><term>Nonpolarized</term><term>Plasma membrane</term><term>Plastic dishes</term><term>Postinfection</term><term>Primary agmk cells</term><term>Recombinant</term><term>Rodriguez</term><term>Rodriguez boulan</term><term>Roth</term><term>Surface expression</term><term>Surface glycoproteins</term><term>Tight junctions</term><term>Vesicular stomatitis virus</term><term>Viral</term><term>Viral glycoproteins</term><term>Virion</term><term>Virus</term><term>Virus maturation</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Primary cell cultures of African Green monkey kidney (AGMK) contain polarized epithelial cells in which influenza virus matures predominantly at the apical surfaces above tight junctions. Influenza virus glycoproteins were found to be localized at the same membrane domain from which the virus budded. When polarized primary AGMK cells were infected with recombinant SV40 viruses containing DNA coding for either an influenza virus H1 or H2 subtype hemagglutinin (HA), the HA proteins were preferentially expressed at the apical surface in a manner identical to that observed in influenza virus-infected cells. Thus, cellular mechanisms for sorting membrane glycoproteins recognize some structural feature of the HA glycoprotein itself, and other viral proteins are not necessary for this process.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Alabama</li><li>Californie</li><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="Alabama"><name sortKey="Roth, Michael G" sort="Roth, Michael G" uniqKey="Roth M" first="Michael G." last="Roth">Michael G. 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