Antigenic modules in the N-terminal S1 region of the transmissible gastroenteritis virus spike protein.
Identifieur interne : 002278 ( Ncbi/Curation ); précédent : 002277; suivant : 002279Antigenic modules in the N-terminal S1 region of the transmissible gastroenteritis virus spike protein.
Auteurs : Juan Reguera [Espagne] ; Desiderio Ordo O [Espagne] ; César Santiago [Espagne] ; Luis Enjuanes [Espagne] ; José M. Casasnovas [Espagne]Source :
- The Journal of general virology [ 1465-2099 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Lignée cellulaire, Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (métabolisme), Structure tertiaire des protéines, Virus de la gastroentérite transmissible (immunologie), Épitopes (immunologie).
- MESH :
- immunologie : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de la gastroentérite transmissible, Épitopes.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux.
- Animaux, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Lignée cellulaire, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Animals, CD13 Antigens (metabolism), Cell Line, Epitopes (immunology), Humans, Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Protein Binding, Protein Structure, Tertiary, Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus, Transmissible gastroenteritis virus (immunology), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , immunology : Epitopes, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : CD13 Antigens, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- immunology : Transmissible gastroenteritis virus.
- Animals, Cell Line, Humans, Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus.
Abstract
The N-terminal S1 region of the transmissible gastroenteritis virus (TGEV) spike (S) glycoprotein contains four antigenic sites (C, B, D and A, from the N- to the C-terminal end) and is engaged in host-cell receptor recognition. The most N-terminal portion of the S1 region, which comprises antigenic sites C and B, is needed for the enteric tropism of TGEV, whereas the major antigenic site A at the C-terminal moiety is required for both respiratory and enteric cell tropism, and is engaged in recognition of the aminopeptidase N (APN) receptor. This study determined the kinetics for binding of a soluble S1 protein to the APN protein. Moreover, the S1 region of the TGEV S protein was dissected, with the aim of identifying discrete modules displaying unique antigenic sites and receptor-binding functions. Following protease treatments and mammalian cell expression methods, four modules or domains (D1-D4) were defined at the S1 region. Papain treatment identified an N-terminal domain (D1) resistant to proteolysis, whereas receptor binding defined a soluble and functional APN receptor-binding domain (D3). This domain was recognized by neutralizing antibodies belonging to the antigenic site A and therefore could be used as an immunogen for the prevention of viral infection. The organization of the four modules in the S1 region of the TGEV S glycoprotein is discussed.
DOI: 10.1099/vir.0.027607-0
PubMed: 21228126
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pubmed:21228126Le document en format XML
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Casasnovas</name><affiliation wicri:level="2"><nlm:affiliation>Department of Macromolecule Structure, Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Darwin 3, 28049 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Department of Macromolecule Structure, Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Darwin 3, 28049 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author></analytic><series><title level="j">The Journal of general virology</title><idno type="eISSN">1465-2099</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>CD13 Antigens (metabolism)</term><term>Cell Line</term><term>Epitopes (immunology)</term><term>Humans</term><term>Membrane Glycoproteins (immunology)</term><term>Membrane Glycoproteins (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Receptors, Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Transmissible gastroenteritis virus (immunology)</term><term>Viral Envelope Proteins (immunology)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (immunologie)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale (immunologie)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Récepteurs viraux (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Virus de la gastroentérite transmissible (immunologie)</term><term>Épitopes (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Epitopes</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>CD13 Antigens</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Virus de la gastroentérite transmissible</term><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The N-terminal S1 region of the transmissible gastroenteritis virus (TGEV) spike (S) glycoprotein contains four antigenic sites (C, B, D and A, from the N- to the C-terminal end) and is engaged in host-cell receptor recognition. The most N-terminal portion of the S1 region, which comprises antigenic sites C and B, is needed for the enteric tropism of TGEV, whereas the major antigenic site A at the C-terminal moiety is required for both respiratory and enteric cell tropism, and is engaged in recognition of the aminopeptidase N (APN) receptor. This study determined the kinetics for binding of a soluble S1 protein to the APN protein. Moreover, the S1 region of the TGEV S protein was dissected, with the aim of identifying discrete modules displaying unique antigenic sites and receptor-binding functions. Following protease treatments and mammalian cell expression methods, four modules or domains (D1-D4) were defined at the S1 region. Papain treatment identified an N-terminal domain (D1) resistant to proteolysis, whereas receptor binding defined a soluble and functional APN receptor-binding domain (D3). This domain was recognized by neutralizing antibodies belonging to the antigenic site A and therefore could be used as an immunogen for the prevention of viral infection. The organization of the four modules in the S1 region of the TGEV S glycoprotein is discussed.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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