Hemagglutination mediated by the spike protein of cell-adapted bovine torovirus.
Identifieur interne : 002621 ( Ncbi/Merge ); précédent : 002620; suivant : 002622Hemagglutination 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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001250
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Links to Exploration step
pubmed:23420207Le document en format XML
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<term>Glycoprotéines membranaires (métabolisme)</term>
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<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>
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<name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name>
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