About: HPV caught in the tetraspanin web?

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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	HPV caught in the tetraspanin web?
Creator	Boller, Klaus Lang, Thorsten Finke, Jérôme Hitschler, Lisa Florin, ·
source	Medline; PMC
abstract	Tetraspanins are master organizers of the cell membrane. Recent evidence suggests that tetraspanins themselves may become crowded by virus particles and that these crowds/aggregates co-internalize with the viral particles. Using microscopy, we studied human papillomavirus (HPV) type 16-dependent aggregates on the cell surface of tetraspanin overexpressing keratinocytes. We find that aggregates are (1) rich in at least two different tetraspanins, (2) three-dimensional architectures extending up to several micrometers into the cell, and (3) decorated intracellularly by filamentous actin. Moreover, in cells not overexpressing tetraspanins, we note that obscurin-like protein 1 (OBSL1), which is thought to be a cytoskeletal adaptor, associates with filamentous actin. We speculate that HPV contact with the cell membrane could trigger the formation of a large tetraspanin web. This web may couple the virus contact site to the intracellular endocytic actin machinery, possibly involving the cytoskeletal adaptor protein OBSL1. Functionally, such a tetraspanin web could serve as a virus entry platform, which is co-internalized with the virus particle. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00430-020-00683-1) contains supplementary material, which is available to authorized users.
has issue date	2020-06-13(xsd:dateTime)
bibo:doi	10.1007/s00430-020-00683-1
bibo:pmid	32535702
has license	cc-by
sha1sum (hex)	af9a7d242d7925dc5ef8f331e0840f3227c1690f
schema:url	https://doi.org/10.1007/s00430-020-00683-1
resource representing a document's title	HPV caught in the tetraspanin web?
has PubMed Central identifier	PMC7293171
has PubMed identifier	32535702
schema:publication	Med Microbiol Immunol
resource representing a document's body	covid:af9a7d242d7925dc5ef8f331e0840f3227c1690f#body_text
is schema:about of	named entity 'tetraspanin' named entity 'cell membrane' named entity 'adaptor' named entity 'contact' named entity 'actin' named entity 'tetraspanin' named entity 'VIRUS PARTICLE' named entity 'HUMAN PAPILLOMAVIRUS ' named entity 'HPV' named entity 'EXTENDING' named entity 'THOUGHT' named entity 'CROWDS' named entity 'TYPE' named entity 'CELLS' named entity 'DECORATED' named entity 'web' named entity 'site' named entity 'contact' named entity 'formation' named entity 'This' named entity 'web' named entity 'cell membrane' named entity 'cytoskeletal' named entity 'large' named entity 'actin' named entity 'keratinocytes' named entity 'machinery' named entity 'speculate' named entity 'web' named entity 'actin' named entity 'virus entry' named entity 'filamentous actin' named entity 'obscurin' named entity 'viral particles' named entity 'protein' named entity 'HPV' named entity 'coronavirus' named entity 'PBS' named entity 'multivesicular bodies' named entity '1:200' named entity 'actin' named entity 'fixed and stained' named entity 'OBSL1' named entity 'CD63' named entity 'growth medium' named entity 'CD63' named entity 'actin' named entity 'actin' named entity 'CD63' named entity 'intracellular' named entity 'HeLa' named entity 'Cell-cell' named entity 'grow larger' named entity 'ROIs' named entity 'CD151' named entity 'microscopy' named entity 'CD151' named entity 'OBSL1' named entity 'actin polymerization' named entity 'adhesion' named entity 'transfection' named entity 'primary antibody' named entity 'intracellular trafficking' named entity 'GFP' named entity 'cell-cell' named entity 'CD63' named entity 'GFP' named entity 'GFP' named entity 'actin' named entity 'HeLa' named entity 'viral entry' named entity 'STED microscopy' named entity 'intracellular trafficking' named entity 'Creative Commons Attribution 4.0' named entity 'adaptor protein' named entity 'RFP' named entity 'cell membrane'

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