About: Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization
Creator	Bederka, Lydia Bonhomme, Cyrille Buchmeier, Michael Ling, Emily
Source	PMC
abstract	The rodent arenavirus glycoprotein complex encodes a stable signal peptide (SSP) that is an essential structural component of mature virions. The SSP, GP1, and GP2 subunits of the trimeric glycoprotein complex noncovalently interact to stud the surface of virions and initiate arenavirus infectivity. Nascent glycoprotein production undergoes two proteolytic cleavage events: first within the endoplasmic reticulum (ER) to cleave SSP from the remaining precursor GP1/2 (glycoprotein complex [GPC]) glycoprotein and second within the Golgi stacks by the cellular SKI-1/S1P for GP1/2 processing to yield GP1 and GP2 subunits. Cleaved SSP is not degraded but retained as an essential glycoprotein subunit. Here, we defined functions of the 58-amino-acid lymphocytic choriomeningitis virus (LCMV) SSP in regard to glycoprotein complex processing and maturation. Using molecular biology techniques, confocal microscopy, and flow cytometry, we detected SSP at the plasma membrane of transfected cells. Further, we identified a sorting signal (FLLL) near the carboxyl terminus of SSP that is required for glycoprotein maturation and trafficking. In the absence of SSP, the glycoprotein accumulated within the ER and was unable to undergo processing by SKI-1/S1P. Mutation of this highly conserved FLLL motif showed impaired glycoprotein processing and secretory pathway trafficking, as well as defective surface expression and pH-dependent membrane fusion. Immunoprecipitation of SSP confirmed an interaction between the signal peptide and the GP2 subunit; however, mutations within this FLLL motif disrupted the association of the GP1 subunit with the remaining glycoprotein complex.
has issue date	2014-10-28(xsd:dateTime)
bibo:doi	10.1128/mbio.02063-14
bibo:pmid	25352624
has license	cc-by-nc-sa
sha1sum (hex)	ab312eb3286e189488707ea7ac8551401a178940
schema:url	https://doi.org/10.1128/mbio.02063-14
resource representing a document's title	Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization
has PubMed Central identifier	PMC4217180
has PubMed identifier	25352624
schema:publication	mBio
resource representing a document's body	covid:ab312eb3286e189488707ea7ac8551401a178940#body_text
is schema:about of	named entity 'glycoprotein' named entity 'maturation' named entity 'SSP' named entity 'expression' named entity 'functions' named entity 'disrupted' named entity 'proteolytic cleavage' named entity 'Further' named entity 'GP2' named entity 'essential' named entity 'sorting signal' named entity 'Glycoprotein' covid:arg/ab312eb3286e189488707ea7ac8551401a178940 named entity 'highly' named entity 'identified' named entity 'SSP' named entity 'Immunoprecipitation' named entity 'complex' named entity 'SSP' named entity 'events' named entity 'SKI' named entity 'subunit' named entity 'regard' named entity 'plasma membrane' named entity 'flow cytometry' named entity 'detected' named entity 'initiate' named entity 'maturation' named entity 'subunit' named entity 'S1P' named entity 'secretory pathway' named entity 'conserved' named entity 'SKI' named entity 'rodent' named entity 'virions' named entity 'GP2' named entity 'motif' named entity 'proteolytic cleavage' named entity 'S1P' named entity 'infectivity' named entity 'motif' named entity 'GP2' named entity 'signal peptide' named entity 'Immunoprecipitation' named entity 'glycoprotein' named entity 'plasma membrane' named entity 'highly conserved' named entity 'Glycoprotein' named entity 'complex' named entity 'expression levels' named entity 'wild-type' named entity 'glycoprotein' named entity 'glycoprotein' named entity 'signal peptide' named entity 'hydrophobic' named entity 'conformational change' named entity 'intracellular transport' named entity 'siRNA' named entity 'motif' named entity 'GP2' named entity 'GP2' named entity 'protein' named entity 'virion' named entity 'GP2' named entity 'GP2' named entity 'hydrophobic' named entity 'C-terminus' named entity 'myristoylation' named entity 'Triton X-100' named entity 'GP2' named entity 'recognition site' named entity '37°C' named entity 'BHK' named entity 'GP2' named entity 'signal peptidase' named entity 'infection' named entity 'protein expression' named entity 'Immunoprecipitation'

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