Hemagglutination mediated by the spike protein of cell-adapted bovine torovirus.
Identifieur interne : 001170 ( PubMed/Checkpoint ); précédent : 001169; suivant : 001171Hemagglutination mediated by the spike protein of cell-adapted bovine torovirus.
Auteurs : Kozue Shimabukuro [Japon] ; Makoto Ujike ; Toshihiro Ito ; Hiroshi Tsunemitsu ; Hitoshi Oshitani ; Fumihiro TaguchiSource :
- Archives of virology [ 1432-8798 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Facteurs de virulence, Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- pathogénicité : Torovirus.
- virologie : Érythrocytes.
- Animaux, Attachement viral, Glycoprotéine de spicule des coronavirus, Hémagglutination.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Virulence Factors.
- pathogenicity : Torovirus.
- virology : Erythrocytes.
- Animals, Hemagglutination, Spike Glycoprotein, Coronavirus, Virus Attachment.
Abstract
Bovine torovirus (BToV)-Aichi, recently isolated in cultured cells, showed hemagglutination (HA) activity, although the virus has a truncated hemagglutinin-esterase (HE) protein, judging from its gene structure, indicating the existence of another viral protein with HA activity. We examined whether the spike (S) protein possesses HA activity. A BToV antiserum used in this study, reactive to S but not to HE, inhibited HA activity. Furthermore, cells infected with BToV and those expressing S showed hemadsorption (HAD) activity, which was inhibited by the anti-BToV serum; however, HAD activity by expressed HE was not blocked. These data indicate that the S protein of BToV-Aichi is responsible for its HA activity.
DOI: 10.1007/s00705-013-1636-4
PubMed: 23420207
Affiliations:
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xml:lang="fr"><term>Animaux</term><term>Attachement viral</term><term>Glycoprotéine de spicule des coronavirus</term><term>Hémagglutination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Bovine torovirus (BToV)-Aichi, recently isolated in cultured cells, showed hemagglutination (HA) activity, although the virus has a truncated hemagglutinin-esterase (HE) protein, judging from its gene structure, indicating the existence of another viral protein with HA activity. We examined whether the spike (S) protein possesses HA activity. A BToV antiserum used in this study, reactive to S but not to HE, inhibited HA activity. Furthermore, cells infected with BToV and those expressing S showed hemadsorption (HAD) activity, which was inhibited by the anti-BToV serum; however, HAD activity by expressed HE was not blocked. These data indicate that the S protein of BToV-Aichi is responsible for its HA activity. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23420207</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-8798</ISSN><JournalIssue CitedMedium="Internet"><Volume>158</Volume><Issue>7</Issue><PubDate><Year>2013</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Archives of virology</Title><ISOAbbreviation>Arch. Virol.</ISOAbbreviation></Journal><ArticleTitle>Hemagglutination mediated by the spike protein of cell-adapted bovine torovirus.</ArticleTitle><Pagination><MedlinePgn>1561-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00705-013-1636-4</ELocationID><Abstract><AbstractText>Bovine torovirus (BToV)-Aichi, recently isolated in cultured cells, showed hemagglutination (HA) activity, although the virus has a truncated hemagglutinin-esterase (HE) protein, judging from its gene structure, indicating the existence of another viral protein with HA activity. We examined whether the spike (S) protein possesses HA activity. A BToV antiserum used in this study, reactive to S but not to HE, inhibited HA activity. Furthermore, cells infected with BToV and those expressing S showed hemadsorption (HAD) activity, which was inhibited by the anti-BToV serum; however, HAD activity by expressed HE was not blocked. 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ValidYN="Y"><LastName>Taguchi</LastName><ForeName>Fumihiro</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>02</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Austria</Country><MedlineTA>Arch Virol</MedlineTA><NlmUniqueID>7506870</NlmUniqueID><ISSNLinking>0304-8608</ISSNLinking></MedlineJournalInfo><ChemicalList><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, 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sortKey="Ujike, Makoto" sort="Ujike, Makoto" uniqKey="Ujike M" first="Makoto" last="Ujike">Makoto Ujike</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Shimabukuro, Kozue" sort="Shimabukuro, Kozue" uniqKey="Shimabukuro K" first="Kozue" last="Shimabukuro">Kozue Shimabukuro</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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