About: Early Porcine Sapovirus Infection Disrupts Tight Junctions and Uses Occludin as a Coreceptor

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About: Early Porcine Sapovirus Infection Disrupts Tight Junctions and Uses Occludin as a Coreceptor Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Early Porcine Sapovirus Infection Disrupts Tight Junctions and Uses Occludin as a Coreceptor
Creator	Cho, Kyoung-Oh Kang, Mun-Il Park, Sang-Ik Kim, Deok-Song Park, Jun-Gyu Baek, Yeong-Bin Cho, Eun-Hyo Kim, Ji-Yun Soliman, Mahmoud Park, Chul-Ho Alfajaro, Mia
Source	Medline; PMC
abstract	The genus Sapovirus belongs to the family Caliciviridae, and its members are common causative agents of severe acute gastroenteritis in both humans and animals. Some caliciviruses are known to use either terminal sialic acids or histo-blood group antigens as attachment factors and/or cell surface proteins, such as CD300lf, CD300ld, and junctional adhesion molecule 1 of tight junctions (TJs), as receptors. However, the roles of TJs and their proteins in sapovirus entry have not been examined. In this study, we found that porcine sapovirus (PSaV) significantly decreased transepithelial electrical resistance and increased paracellular permeability early in infection of LLC-PK cells, suggesting that PSaV dissociates TJs of cells. This led to the interaction between PSaV particles and occludin, which traveled in a complex into late endosomes via Rab5- and Rab7-dependent trafficking. Inhibition of occludin using small interfering RNA (siRNA), a specific antibody, or a dominant-negative mutant significantly blocked the entry of PSaV. Transient expression of occludin in nonpermissive Chinese hamster ovary (CHO) cells conferred susceptibility to PSaV, but only for a limited time. Although claudin-1, another TJ protein, neither directly interacted nor was internalized with PSaV particles, it facilitated PSaV entry and replication in the LLC-PK cells. We conclude that PSaV particles enter LLC-PK cells by binding to occludin as a coreceptor in PSaV-dissociated TJs. PSaV and occludin then form a complex that moves to late endosomes via Rab5- and Rab7-dependent trafficking. In addition, claudin-1 in the TJs opened by PSaV infection facilitates PSaV entry and infection as an entry factor. IMPORTANCE Sapoviruses (SaVs) cause severe acute gastroenteritis in humans and animals. Although they replicate in intestinal epithelial cells, which are tightly sealed by apical-junctional complexes, such as tight junctions (TJs), the mechanisms by which SaVs hijack TJs and their proteins for successful entry and infection remain largely unknown. Here, we demonstrate that porcine SaVs (PSaVs) induce early dissociation of TJs, allowing them to bind to the TJ protein occludin as a functional coreceptor. PSaVs then travel in a complex with occludin into late endosomes through Rab5- and Rab7-dependent trafficking. Claudin-1, another TJ protein, does not directly interact with PSaV but facilitates the entry of PSaV into cells as an entry factor. This work contributes to our understanding of the entry of SaV and other caliciviruses into cells and may aid in the development of efficient and affordable drugs to treat SaV infections.
has issue date	2019-02-05(xsd:dateTime)
bibo:doi	10.1128/jvi.01773-18
bibo:pmid	30463963
has license	cc-by
sha1sum (hex)	2c6d57a5c31e345cd689687255b13506d71df902
schema:url	https://doi.org/10.1128/jvi.01773-18
resource representing a document's title	Early Porcine Sapovirus Infection Disrupts Tight Junctions and Uses Occludin as a Coreceptor
has PubMed Central identifier	PMC6364031
has PubMed identifier	30463963
schema:publication	J Virol
resource representing a document's body	covid:2c6d57a5c31e345cd689687255b13506d71df902#body_text
is schema:about of	named entity 'small interfering RNA' named entity 'complex' named entity 'occludin' named entity 'siRNA' named entity 'sialic acids' named entity 'Rab5' named entity 'replicate' named entity 'hijack' named entity 'antibody' named entity 'moves' named entity 'antigens' named entity 'SMALL INTERFERING RNA' named entity 'CORECEPTOR' named entity 'FORM' named entity 'ENDOSOMES' named entity 'DIRECTLY' named entity 'EARLY' named entity 'CONCLUDE' named entity 'EXAMINED' named entity 'THEIR' named entity 'DOES NOT' named entity 'COMPLEX' named entity 'JUNCTIONAL COMPLEXES' named entity 'KNOWN' named entity 'HAVE' named entity 'RAB7' named entity 'SAV' named entity 'INHIBITION' named entity 'BINDING' named entity 'INTESTINAL' named entity 'PROTEINS' named entity 'ATTACHMENT' named entity 'DISSOCIATION' named entity 'OPENED' named entity 'GENUS SAPOVIRUS' named entity 'RAB5' named entity 'TRAVEL' named entity 'UNKNOWN' named entity 'PARTICLES' named entity 'CHINESE HAMSTER' named entity 'ALLOWING' named entity 'SURFACE PROTEINS' named entity 'CAUSATIVE AGENTS' named entity 'INTERACTION' named entity 'OVARY' named entity 'PORCINE' named entity 'FAMILY CALICIVIRIDAE' named entity 'OCCLUDIN' named entity 'ANTIGENS' named entity 'LIMITED TIME' named entity 'AID' named entity 'TERMINAL' named entity 'SEVERE' named entity 'HERE' named entity 'APICAL' named entity 'CELL SURFACE' named entity 'LED' named entity 'USE' named entity 'SAPOVIRUS' named entity 'DEPENDENT' named entity 'TO BIND TO' named entity 'STUDY' named entity 'CAUSE' named entity 'HUMANS' named entity 'CELLS' named entity 'MEMBERS' named entity 'ADDITION' named entity 'DECREASED' named entity 'CD300LF' named entity 'PORCINE' named entity 'ENTRY'

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