About: Tubulins interact with porcine and human S proteins of the genus Alphacoronavirus and support successful assembly and release of infectious viral particles

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About: Tubulins interact with porcine and human S proteins of the genus Alphacoronavirus and support successful assembly and release of infectious viral particles Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Tubulins interact with porcine and human S proteins of the genus Alphacoronavirus and support successful assembly and release of infectious viral particles
Creator	Ma-Lauer, Yue Schwegmann-Weßels, Christel Mayrhofer, Peter Müthing, Johannes Pohlentz, Gottfried Rüdiger, Anna-Theresa Von Brunn, Albrecht
source	Elsevier; Medline; PMC
abstract	Abstract Coronavirus spike proteins mediate host-cell-attachment and virus entry. Virus replication takes place within the host cell cytosol, whereas assembly and budding occur at the endoplasmic reticulum-Golgi intermediate compartment. In this study we demonstrated that the last 39 amino acid stretches of Alphacoronavirus spike cytoplasmic domains of the human coronavirus 229E, NL63, and the porcine transmissible gastroenteritis virus TGEV interact with tubulin alpha and beta chains. In addition, a partial co-localization of TGEV spike proteins with authentic host cell β-tubulin was observed. Furthermore, drug-induced microtubule depolymerization led to changes in spike protein distribution, a reduction in the release of infectious virus particles and less amount of spike protein incorporated into virions. These data demonstrate that interaction of Alphacoronavirus spike proteins with tubulin supports S protein transport and incorporation into virus particles.
has issue date	2016-10-31(xsd:dateTime)
bibo:doi	10.1016/j.virol.2016.07.022
bibo:pmid	27479465
has license	els-covid
sha1sum (hex)	f3b41989daa6eba33f6224f9555a07d398d05dd2
schema:url	https://doi.org/10.1016/j.virol.2016.07.022
resource representing a document's title	Tubulins interact with porcine and human S proteins of the genus Alphacoronavirus and support successful assembly and release of infectious viral particles
has PubMed Central identifier	PMC7111311
has PubMed identifier	27479465
schema:publication	Virology
resource representing a document's body	covid:f3b41989daa6eba33f6224f9555a07d398d05dd2#body_text
is schema:about of	named entity 'porcine' named entity 'budding' named entity 'observed' named entity 'porcine' covid:arg/f3b41989daa6eba33f6224f9555a07d398d05dd2 named entity 'particles' named entity 'tubulin' named entity 'replication' named entity 'β-tubulin' named entity 'domains' named entity 'cytosol' named entity 'virus' named entity 'spike' named entity 'stretches' named entity 'interact' named entity 'drug-induced' named entity 'Virus replication' named entity 'β-tubulin' named entity 'virus' named entity 'host-cell' named entity 'porcine' named entity 'human coronavirus' named entity 'amino acid' named entity 'viral particles' named entity 'porcine' named entity 'genus' named entity 'study' named entity 'S protein' named entity 'marker proteins' named entity 'protein' named entity 'Leica' named entity 'transfected' named entity 'fetal calf serum' named entity 'motor proteins' named entity 'tubulin' named entity 'plaque forming units' named entity 'lysed' named entity 'tyrosine' named entity 'hpi' named entity 'GFP' named entity 'motif' named entity 'C-terminally' named entity 'protein localization' named entity 'tubulins' named entity 'supernatant' named entity 'functional analysis' named entity 'hpi' named entity 'white arrows' named entity 'kinesin' named entity 'HCoV-229E' named entity 'HCoV NL63' named entity 'acetonitrile' named entity 'pull down assay' named entity 'TGEV' named entity 'infection' named entity 'TGEV' named entity 'NP-40' named entity 'antibody' named entity 'infection control' named entity 'plasma membrane' named entity 'host cell' named entity 'cytoplasmic' named entity 'cytotoxic' named entity 'secretory pathway' named entity 'supernatants' named entity 'nucleocapsid' named entity 'feline infectious peritonitis virus' named entity 'Betacoronavirus' named entity 'transcription' named entity 'ERGIC' named entity 'HEK-293' named entity 'vimentin' named entity 'cell surface' named entity 'TGEV' named entity 'expression patterns'

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