Peptide nanoparticles as novel immunogens: design and analysis of a prototypic severe acute respiratory syndrome vaccine.
Identifieur interne : 002A58 ( Main/Exploration ); précédent : 002A57; suivant : 002A59Peptide nanoparticles as novel immunogens: design and analysis of a prototypic severe acute respiratory syndrome vaccine.
Auteurs : Tais A P F. Pimentel [États-Unis] ; Zhe Yan ; Scott A. Jeffers ; Kathryn V. Holmes ; Robert S. Hodges ; Peter BurkhardSource :
- Chemical biology & drug design [ 1747-0285 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Anticorps (immunologie), Conformation des protéines, Données de séquences moléculaires, Humains, Modèles moléculaires, Nanoparticules (), Nanoparticules (ultrastructure), Peptides (), Peptides (génétique), Peptides (immunologie), Protéines de fusion recombinantes (), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Similitude de séquences d'acides aminés, Souris, Souris de lignée BALB C, Sous-unités de protéines (), Sous-unités de protéines (immunologie), Syndrome respiratoire aigu sévère (), Syndrome respiratoire aigu sévère (immunologie), Séquence d'acides aminés, Test ELISA (), Vaccins (), Vaccins (immunologie), Virus du SRAS (immunologie), Épitopes (), Épitopes (immunologie).
- MESH :
- génétique : Peptides, Protéines de fusion recombinantes.
- immunologie : Anticorps, Peptides, Sous-unités de protéines, Syndrome respiratoire aigu sévère, Vaccins, Virus du SRAS, Épitopes.
- métabolisme : Protéines de fusion recombinantes.
- Animaux, Conformation des protéines, Données de séquences moléculaires, Humains, Modèles moléculaires, Nanoparticules, Peptides, Protéines de fusion recombinantes, Similitude de séquences d'acides aminés, Souris, Souris de lignée BALB C, Sous-unités de protéines, Syndrome respiratoire aigu sévère, Séquence d'acides aminés, Test ELISA, Vaccins, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies (immunology), Enzyme-Linked Immunosorbent Assay (methods), Epitopes (chemistry), Epitopes (immunology), Humans, Mice, Mice, Inbred BALB C, Models, Molecular, Molecular Sequence Data, Nanoparticles (chemistry), Nanoparticles (ultrastructure), Peptides (chemistry), Peptides (genetics), Peptides (immunology), Protein Conformation, Protein Subunits (chemistry), Protein Subunits (immunology), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (immunology), Sequence Homology, Amino Acid, Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (prevention & control), Vaccines (chemistry), Vaccines (immunology).
- MESH :
- chemical , chemistry : Epitopes, Peptides, Protein Subunits, Recombinant Fusion Proteins, Vaccines.
- chemical , genetics : Peptides, Recombinant Fusion Proteins.
- chemical , immunology : Antibodies, Epitopes, Peptides, Protein Subunits, Vaccines.
- chemistry : Nanoparticles.
- immunology : SARS Virus, Severe Acute Respiratory Syndrome.
- chemical , metabolism : Recombinant Fusion Proteins.
- methods : Enzyme-Linked Immunosorbent Assay.
- prevention & control : Severe Acute Respiratory Syndrome.
- ultrastructure : Nanoparticles.
- Amino Acid Sequence, Animals, Humans, Mice, Mice, Inbred BALB C, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid.
Abstract
Severe acute respiratory syndrome (SARS) is an infectious disease caused by a novel coronavirus that cost nearly 800 lives. While there have been no recent outbreaks of the disease, the threat remains as SARS coronavirus (SARS-CoV) like strains still exist in animal reservoirs. Therefore, the development of a vaccine against SARS is in grave need. Here, we have designed and produced a prototypic SARS vaccine: a self-assembling polypeptide nanoparticle that repetitively displays a SARS B-cell epitope from the C-terminal heptad repeat of the virus' spike protein. Biophysical analyses with circular dichroism, transmission electron microscopy and dynamic light scattering confirmed the computational design showing alpha-helcial nanoparticles with sizes of about 25 nm. Immunization experiments with no adjuvants were performed with BALB/c mice. An investigation of the binding properties of the elicited antibodies showed that they were highly conformation specific for the coiled-coil epitope because they specifically recognized the native trimeric conformation of C-terminal heptad repeat region. Consequently, the antisera exhibited neutralization activity in an in vitro infection inhibition assay. We conclude that these peptide nanoparticles represent a promising platform for vaccine design, in particular for diseases that are characterized by neutralizing epitopes with coiled-coil conformation such as SARS-CoV or other enveloped viruses.
DOI: 10.1111/j.1747-0285.2008.00746.x
PubMed: 19152635
Affiliations:
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Le document en format XML
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Conformation</term><term>Protein Subunits (chemistry)</term><term>Protein Subunits (immunology)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (immunology)</term><term>Sequence Homology, Amino Acid</term><term>Severe Acute Respiratory Syndrome (immunology)</term><term>Severe Acute Respiratory Syndrome (prevention & control)</term><term>Vaccines (chemistry)</term><term>Vaccines (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps (immunologie)</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Modèles moléculaires</term><term>Nanoparticules ()</term><term>Nanoparticules (ultrastructure)</term><term>Peptides ()</term><term>Peptides (génétique)</term><term>Peptides (immunologie)</term><term>Protéines de fusion recombinantes 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moléculaires</term><term>Nanoparticules</term><term>Peptides</term><term>Protéines de fusion recombinantes</term><term>Similitude de séquences d'acides aminés</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Sous-unités de protéines</term><term>Syndrome respiratoire aigu sévère</term><term>Séquence d'acides aminés</term><term>Test ELISA</term><term>Vaccins</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an infectious disease caused by a novel coronavirus that cost nearly 800 lives. While there have been no recent outbreaks of the disease, the threat remains as SARS coronavirus (SARS-CoV) like strains still exist in animal reservoirs. Therefore, the development of a vaccine against SARS is in grave need. Here, we have designed and produced a prototypic SARS vaccine: a self-assembling polypeptide nanoparticle that repetitively displays a SARS B-cell epitope from the C-terminal heptad repeat of the virus' spike protein. Biophysical analyses with circular dichroism, transmission electron microscopy and dynamic light scattering confirmed the computational design showing alpha-helcial nanoparticles with sizes of about 25 nm. Immunization experiments with no adjuvants were performed with BALB/c mice. An investigation of the binding properties of the elicited antibodies showed that they were highly conformation specific for the coiled-coil epitope because they specifically recognized the native trimeric conformation of C-terminal heptad repeat region. Consequently, the antisera exhibited neutralization activity in an in vitro infection inhibition assay. We conclude that these peptide nanoparticles represent a promising platform for vaccine design, in particular for diseases that are characterized by neutralizing epitopes with coiled-coil conformation such as SARS-CoV or other enveloped viruses.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Connecticut</li></region></list><tree><noCountry><name sortKey="Burkhard, Peter" sort="Burkhard, Peter" uniqKey="Burkhard P" first="Peter" last="Burkhard">Peter Burkhard</name><name sortKey="Hodges, Robert S" sort="Hodges, Robert S" uniqKey="Hodges R" first="Robert S" last="Hodges">Robert S. Hodges</name><name sortKey="Holmes, Kathryn V" sort="Holmes, Kathryn V" uniqKey="Holmes K" first="Kathryn V" last="Holmes">Kathryn V. Holmes</name><name sortKey="Jeffers, Scott A" sort="Jeffers, Scott A" uniqKey="Jeffers S" first="Scott A" last="Jeffers">Scott A. Jeffers</name><name sortKey="Yan, Zhe" sort="Yan, Zhe" uniqKey="Yan Z" first="Zhe" last="Yan">Zhe Yan</name></noCountry><country name="États-Unis"><region name="Connecticut"><name sortKey="Pimentel, Tais A P F" sort="Pimentel, Tais A P F" uniqKey="Pimentel T" first="Tais A P F" last="Pimentel">Tais A P F. Pimentel</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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