About: Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT‐independent manner

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About: Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT‐independent manner 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
has title	Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT‐independent manner
Creator	Döring, Tatjana Prange, Reinhild Stieler, Jens Bardens, Andreas
Source	Medline; PMC
abstract	Hepatitis B virus (HBV) is an enveloped DNA virus that exploits the endosomal sorting complexes required for transport (ESCRT) pathway for budding. In addition to infectious particles, HBV‐replicating cells release non‐enveloped (nucleo)capsids, but their functional implication and pathways of release are unclear. Here, we focused on the molecular mechanisms and found that the sole expression of the HBV core protein is sufficient for capsid release. Unexpectedly, released capsids are devoid of a detectable membrane bilayer, implicating a non‐vesicular exocytosis process. Unlike virions, naked capsid budding does not require the ESCRT machinery. Rather, we identified Alix, a multifunctional protein with key roles in membrane biology, as a regulator of capsid budding. Ectopic overexpression of Alix enhanced capsid egress, while its depletion inhibited capsid release. Notably, the loss of Alix did not impair HBV production, furthermore indicating that virions and capsids use diverse export routes. By mapping of Alix domains responsible for its capsid release‐mediating activity, its Bro1 domain was found to be required and sufficient. Alix binds to core via its Bro1 domain and retained its activity even if its ESCRT‐III binding site is disrupted. Together, the boomerang‐shaped Bro1 domain of Alix appears to escort capsids without ESCRT.
has issue date	2010-12-28(xsd:dateTime)
bibo:doi	10.1111/j.1462-5822.2010.01557.x
bibo:pmid	21129143
has license	no-cc
sha1sum (hex)	a4c28f3f9d1698eb8139684c03cd4da613293768
schema:url	https://doi.org/10.1111/j.1462-5822.2010.01557.x
resource representing a document's title	Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT‐independent manner
has PubMed Central identifier	PMC7162389
has PubMed identifier	21129143
schema:publication	Cell Microbiol
resource representing a document's body	covid:a4c28f3f9d1698eb8139684c03cd4da613293768#body_text
is schema:about of	named entity 'ESCRT' named entity 'core' named entity 'membrane biology' named entity 'core' named entity 'Here' named entity 'exocytosis' named entity 'DETECTABLE' named entity 'DOES NOT' named entity 'DIVERSE' named entity 'identified' named entity 'Alix' named entity 'HBV' named entity 'capsid' named entity 'ESCRT' named entity 'Alix' named entity 'capsid' named entity 'protein' named entity 'HBV' named entity 'ESCRT' named entity 'activity' named entity 'virions' named entity 'sorting' named entity 'binding site' named entity 'capsid' named entity 'capsid' named entity 'capsid' named entity 'HBV' named entity 'capsids' named entity 'ESCRT' named entity 'ESCRT' named entity 'cell line' named entity 'capsid' named entity 'capsids' named entity 'non-enveloped' named entity 'cloning' named entity 'transfected' named entity 'produce antibodies' named entity 'capsids' named entity 'glycoprotein' named entity 'culture media' named entity 'fluorescence' named entity 'polyethylene glycol' named entity 'gradient' named entity 'Asp' named entity 'kDa' named entity 'mutagenesis' named entity 'NP-40' named entity 'cell functions' named entity 'capsid' named entity 'nuclei' named entity 'capsid' named entity 'viral DNA' named entity 'immunogenic' named entity 'lytic' named entity 'RNA silencing' named entity 'HBV' named entity 'GFP' named entity 'influenza virus' named entity 'capsids' named entity 'polymerase' named entity 'sucrose' named entity 'capsid' named entity 'siRNA' named entity 'endocytosis' named entity 'Tsg101' named entity 'capsids' named entity 'w/v' named entity 'virus' named entity 'VSV-G' named entity 'Plasmid' named entity 'vesicular stomatitis virus' named entity 'HuH-7' named entity 'colocalization' named entity 'capsid' named entity 'denaturing conditions' named entity 'envelope proteins' named entity 'nucleocapsids' named entity 'dot-blot'

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