Neutralizing epitopes of human parainfluenza virus type 3 are conformational and cannot be imitated by synthetic peptides
Identifieur interne : 004914 ( Main/Exploration ); précédent : 004913; suivant : 004915Neutralizing epitopes of human parainfluenza virus type 3 are conformational and cannot be imitated by synthetic peptides
Auteurs : Kelly J. Henrickson [États-Unis] ; David W. Kingsbury [États-Unis] ; Kathleen L. Van Wyke Coelingh [États-Unis] ; Clayton W. Naeve ; Allen Portner [États-Unis]Source :
- Vaccine [ 0264-410X ] ; 1991.
English descriptors
- Teeft :
- Acid sequence, Amino, Amino acid, Amino acid sequence, Amino acid sequences, Amino acids, Antibody binding, Antigenic, Antigenic variation, Assay, Coelingh, Competition elisa, Elisa, Elisa plates, Epitope, Extramembranous portion, Glycoprotein, Henrickson, Human parainfluenza type, Human parainfluenza virus, Human parainfluenza virus type, Human sera, Infectious diseases, Linear epitope, Linear epitopes, Mabs, Monoclonal antibodies, Mutation, Native conformation, Natl acad, Neutralizing, Neutralizing epitopes, Neutralizing mabs, Parainfluenza, Peptide, Point mutation sites, Respiratory syncytial virus, Room temperature, Serum samples, Surface glycoproteins, Synthetic peptide, Synthetic peptide vaccine, Synthetic peptides, Titre, Vaccine, Viral, Virol, Virology, Virus, Western blot analysis, Wyke, Wyke coelingh.
Abstract
Abstract: The possibility that linear epitopes on the haemagglutinin-neuraminidase (HN) surface glycoprotein of human parainfluenza virus type 3 (PIV-3) might induce neutralizing antibodies after virus infection was investigated. Thirty-seven peptides, representing 64% of the extramembranous portion of the HN molecule of PIV-3, were synthesized. Their ability to bind to 14 neutralizing murine monoclonal antibodies (mAbs) specific for HN or 26 high-titre human serum samples were tested in a direct enzyme-linked immunosorbent assay (ELISA) and in an indirect competition ELISA. None of the synthetic peptides reacted with any of the mAbs or serum samples in the direct test and none of 11 synthetic peptides tested blocked mAbs from binding to HN in the competition ELISA. These findings suggest that synthetic peptides cannot be used to imitate the known neutralizing epitopes on the HN. Analyses of reduced and non-reduced HN in ELISA and immunoblot assays confirmed that protein folding and tertiary structure are essential for epitope formation in these neutralizing sites. However, some children's sera analysed by immunoblotting contained antibodies to an uncharacterized linear epitope(s) not recognized by our panel of mAbs, raising the possibility that a neutralizing linear epitope does exist on the HN of PIV-3.
Url:
DOI: 10.1016/0264-410X(91)90107-H
Affiliations:
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Henrickson</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Infectious Diseases and the Department of Virology and Molecular Biology, St Jude Children's Research Hospital, Memphis, Tennessee</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>∗Present address: Department of Pediatrics, MACC Fund Research Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, Wisconsin 53226</wicri:regionArea><wicri:noRegion>Wisconsin 53226</wicri:noRegion></affiliation></author><author><name sortKey="Kingsbury, David W" sort="Kingsbury, David W" uniqKey="Kingsbury D" first="David W." last="Kingsbury">David W. Kingsbury</name><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>†Present address: Howard Hughes Medical Institute, 6701 Rockledge Drive, Bethesda, MD 20817</wicri:regionArea><wicri:noRegion>MD 20817</wicri:noRegion></affiliation></author><author><name sortKey="Van Wyke Coelingh, Kathleen L" sort="Van Wyke Coelingh, Kathleen L" uniqKey="Van Wyke Coelingh K" first="Kathleen L." last="Van Wyke Coelingh">Kathleen L. Van Wyke Coelingh</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Naeve, Clayton W" sort="Naeve, Clayton W" uniqKey="Naeve C" first="Clayton W." last="Naeve">Clayton W. Naeve</name></author><author><name sortKey="Portner, Allen" sort="Portner, Allen" uniqKey="Portner A" first="Allen" last="Portner">Allen Portner</name><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>To whom correspondence should be addressed, at St Jude Children's Research Hospital, Department of Virology, PO Box 318, Memphis, Tennessee 38101-0318</wicri:regionArea><wicri:noRegion>Tennessee 38101-0318</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Vaccine</title><title level="j" type="abbrev">JVAC</title><idno type="ISSN">0264-410X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">9</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="243">243</biblScope><biblScope unit="page" to="249">249</biblScope></imprint><idno type="ISSN">0264-410X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0264-410X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid sequence</term><term>Amino</term><term>Amino acid</term><term>Amino acid sequence</term><term>Amino acid sequences</term><term>Amino acids</term><term>Antibody binding</term><term>Antigenic</term><term>Antigenic variation</term><term>Assay</term><term>Coelingh</term><term>Competition elisa</term><term>Elisa</term><term>Elisa plates</term><term>Epitope</term><term>Extramembranous portion</term><term>Glycoprotein</term><term>Henrickson</term><term>Human parainfluenza type</term><term>Human parainfluenza virus</term><term>Human parainfluenza virus type</term><term>Human sera</term><term>Infectious diseases</term><term>Linear epitope</term><term>Linear epitopes</term><term>Mabs</term><term>Monoclonal antibodies</term><term>Mutation</term><term>Native conformation</term><term>Natl acad</term><term>Neutralizing</term><term>Neutralizing epitopes</term><term>Neutralizing mabs</term><term>Parainfluenza</term><term>Peptide</term><term>Point mutation sites</term><term>Respiratory syncytial virus</term><term>Room temperature</term><term>Serum samples</term><term>Surface glycoproteins</term><term>Synthetic peptide</term><term>Synthetic peptide vaccine</term><term>Synthetic peptides</term><term>Titre</term><term>Vaccine</term><term>Viral</term><term>Virol</term><term>Virology</term><term>Virus</term><term>Western blot analysis</term><term>Wyke</term><term>Wyke coelingh</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The possibility that linear epitopes on the haemagglutinin-neuraminidase (HN) surface glycoprotein of human parainfluenza virus type 3 (PIV-3) might induce neutralizing antibodies after virus infection was investigated. Thirty-seven peptides, representing 64% of the extramembranous portion of the HN molecule of PIV-3, were synthesized. Their ability to bind to 14 neutralizing murine monoclonal antibodies (mAbs) specific for HN or 26 high-titre human serum samples were tested in a direct enzyme-linked immunosorbent assay (ELISA) and in an indirect competition ELISA. None of the synthetic peptides reacted with any of the mAbs or serum samples in the direct test and none of 11 synthetic peptides tested blocked mAbs from binding to HN in the competition ELISA. These findings suggest that synthetic peptides cannot be used to imitate the known neutralizing epitopes on the HN. Analyses of reduced and non-reduced HN in ELISA and immunoblot assays confirmed that protein folding and tertiary structure are essential for epitope formation in these neutralizing sites. However, some children's sera analysed by immunoblotting contained antibodies to an uncharacterized linear epitope(s) not recognized by our panel of mAbs, raising the possibility that a neutralizing linear epitope does exist on the HN of PIV-3.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li><li>Tennessee</li></region></list><tree><noCountry><name sortKey="Naeve, Clayton W" sort="Naeve, Clayton W" uniqKey="Naeve C" first="Clayton W." last="Naeve">Clayton W. Naeve</name></noCountry><country name="États-Unis"><region name="Tennessee"><name sortKey="Henrickson, Kelly J" sort="Henrickson, Kelly J" uniqKey="Henrickson K" first="Kelly J." last="Henrickson">Kelly J. Henrickson</name></region><name sortKey="Henrickson, Kelly J" sort="Henrickson, Kelly J" uniqKey="Henrickson K" first="Kelly J." last="Henrickson">Kelly J. Henrickson</name><name sortKey="Kingsbury, David W" sort="Kingsbury, David W" uniqKey="Kingsbury D" first="David W." last="Kingsbury">David W. Kingsbury</name><name sortKey="Portner, Allen" sort="Portner, Allen" uniqKey="Portner A" first="Allen" last="Portner">Allen Portner</name><name sortKey="Van Wyke Coelingh, Kathleen L" sort="Van Wyke Coelingh, Kathleen L" uniqKey="Van Wyke Coelingh K" first="Kathleen L." last="Van Wyke Coelingh">Kathleen L. Van Wyke Coelingh</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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